CiteSeerX - Document Details (Isaac Councill, Lee Giles, Pradeep Teregowda): Background The protein structure prediction problem is one of the most challenging problems in biological sciences. Many approaches have been proposed using database information and/or simplified protein models. The protein structure prediction problem can be cast in the form of an optimization problem. Notwithstanding its importance, the problem has very seldom been tackled by Constraint Logic Programming, a declarative programming paradigm suitable for solving combinatorial optimization problems. Results Constraint Logic Programming techniques have been applied to the protein structure prediction problem on the face-centered cube lattice model. Molecular dynamics techniques, endowed with the notion of constraint, have been also exploited. Even using a very simplified model, Constraint Logic Programming on the face-centered cube lattice model allowed us to obtain acceptable results for a few small proteins. As a test
Review Graduate Program details of Biomolecular Structure and Biophysics - Master in West Lafayette Indiana United States from Purdue University. Biomolecular Structure and Biophysics is part of the Purdue University Interdisciplinary Life Science Program (PULSe). Some of the highlights of PULSe include: PULSe offers...
To gain a better understanding of how proteins function a process known as protein structure prediction (PSP) is carried out. However, experimental PSP methods, such as X-ray crystallography and Nuclear Magnetic Resonance (NMR), can be time-consuming and inaccurate. This has given rise to numerous computational PSP approaches to try and elicit a proteins three-dimensional conformation. A popular PSP search strategy is Genetic Algorithms (GA). GAs allow for a generic search approach, which can provide a generic improvement to alleviate the need to redefine the search strategies for separate sequences. Though GAs working principles are remarkable, a serious problem that is inherent in the GA search process is the growth of twins or identical chromosomes. Therefore, enhanced twin removal strategies are crucial for any GA search solving hard-optimisation problems like PSP. In this paper we explain our high-resolution GA feature-based resampling PSP approach and propose a twin removal strategy to ...
Tetracycline-responsive transcriptional activator driven by the liver-specific mouse major urinary protein promoter (MUP-tTA).. The E. Coli tetracycline operon regulatory system was used to generate a liver-specific transcription activation system that was inhibited by tetracycline. The transcription activator was a fused protein consisting of a tetracycline repressor gene (tetR) that was only active in the presence of tetracycline and a herpes simplex virus protein (VP-16) transcription activating domain (Tet-Off). Transcription was induced only in the absence of tetracycline (Tet-Off). A liver-specific promoter such as the mouse major urinary protein (MUP) promoter determined that the tetracycline-regulated transcriptional activator (tTA) would be expressed specifically in liver. To study the effect of the transcription activator on a target gene (for example, beta-galactosidase, LacZ) specifically in liver, MUP-tTA mice would be mated with transgenic mice in which the TAg Target gene was ...
The Protein Model Portal was developed as a module of the Protein Structure Initiative Knowledgebase (PSI KB). The goal of the Models Module was to develop a portal that gave access to the various models that can be leveraged from PSI targets and other experimental protein structures. The Protein Structure Initiative has been successful in determining the structures of many unique proteins in a high throughput manner. Still, the number of known protein sequences is much larger than the number of experimentally solved protein structures. Homology (or comparative) modeling methods make use of experimental protein structures to build models for evolutionary related proteins. Experimental structural biology and homology modeling thereby complement each other in the exploration of the protein structure space.. Reference: Haas J., Roth S., Arnold, K., Kiefer, F., Schmidt T., Bordoli, L. and Schwede, T. (2013). The Protein Model Portal - a comprehensive resource for protein structure and model ...
The Protein Model Portal was developed as a module of the Protein Structure Initiative Knowledgebase (PSI KB). The goal of the Models Module was to develop a portal that gave access to the various models that can be leveraged from PSI targets and other experimental protein structures. The Protein Structure Initiative has been successful in determining the structures of many unique proteins in a high throughput manner. Still, the number of known protein sequences is much larger than the number of experimentally solved protein structures. Homology (or comparative) modeling methods make use of experimental protein structures to build models for evolutionary related proteins. Experimental structural biology and homology modeling thereby complement each other in the exploration of the protein structure space.. Reference: Haas J., Roth S., Arnold, K., Kiefer, F., Schmidt T., Bordoli, L. and Schwede, T. (2013). The Protein Model Portal - a comprehensive resource for protein structure and model ...
Computational protein structure prediction has made great progress in the last three decades [1, 2]. Protein inter-residue contact prediction is one of the problems being actively studied in the structure prediction community. Recent CASP (Critical Assessment of Techniques for Protein Structure Prediction) [3-7] events have demonstrated that a few true contacts, extracted from template-based models, can provide very important information for protein structure refinement, especially on targets without good templates in PDB [8]. For example, Misura et al. [9] have revised the widely-used ab initio folding program, Rosetta [10], by incorporating inter-residue contact information as a component of Rosettas energy function, and shown that the revised Rosetta exhibits not only a better computational efficiency, but also a better prediction accuracy. For some test proteins, the models built by this revised Rosetta are more accurate than their template-based counterparts, which is rarely seen before ...
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Protein three-dimensional structure prediction directly from amino acid sequence is an important issue in bioinformatics. An intermediate approach to this problem is to predict the so-called one-dimensional structural properties of proteins. The solvent accessibility or accessible surface area (ASA) of an amino acid residue in a protein structure is one such property and the knowledge of this property can significantly enhance the overall structure and function prediction of proteins [1, 2]. Given an amino acid sequence, the goal of such prediction is to estimate the ASA of each residue making use of previously observed ASA values taken from known protein structures. The knowledge from previously observed structures is modeled using machine learning and other methods [3-16]. Various methods of predicting ASA from sequence or sequence-derived evolutionary information have been developed such as neural networks [8-12], Bayesian analysis [13], information theory [14, 15], multiple linear ...
Blind protein structure predictions from CASP3 and CASP4. A: Left, crystal structure of the MarA transcription factor bound to DNA; right, our best submitted model in CASP3. Despite many incorrect details, the overall fold is predicted with sufficient accuracy to allow insights into the mode of DNA binding. B: Left, the crystal structure of bacteriocin AS-48; middle, our best submitted model in CASP4; right, a structurally and functionally related protein (NK-lysin) identified using this model in a structure-based search of the Protein Data Bank (PDB). The structural and functional similarity is not recognizable using sequence comparison methods (the identity between the two sequences is only 5 percent). C: Left, crystal structure of the second domain of MutS; middle, our best submitted model for this domain in CASP4; right, a structurally related protein (RuvC) with a related function recognized using the model in a structure-based search of the PDB. The similarity was not recognized using ...
The structure of a protein ultimately determines its function; therefore, knowledge of three-dimensional structure is essential for understanding its function and mechanism of action. The two most common methods for determining protein structure are x-ray crystallography and Nuclear Magnetic Resonance (NMR) spectroscopy. These methods are quite successful but can be very time-intensive and costly. An alternative method is protein structure prediction, where structure is computationally predicted from amino acid sequence. As opposed to x-ray crystallography and NMR spectroscopy, protein structure prediction is not encumbered by potential experimental problems. In this research, we attempted to determine if certain protein structure features, known as tertiary contacts, can improve the prediction of protein three-dimensional structure. By calculating and analyzing sequence homology and related values, it was shown that tertiary contacts, which typically are long-range amino acid interactions
Free Online Library: Analysis of an immune algorithm for protein structure prediction.(Report) by Informatica; Computers and office automation Algorithms Usage Mutation Research Mutation (Biology) Protein folding Methods Models Protein structure Proteins Structure Simulation Simulation methods
Successful protein structure prediction requires accurate low-resolution scoring functions so that protein main chain conformations that are close to the native can be identified. Once that is accomplished, a more detailed and time-consuming treatment to produce all-atom models can be undertaken. The earliest low-resolution scoring used simple distance-based contact potentials, but more recently, the relative orientations of interacting amino acids have been taken into account to improve performance. We developed a new knowledge-based scoring function, LoCo, that locates the interaction partners of each individual residue within a local coordinate system based only on the position of its main chain N, Cα and C atoms. LoCo was trained on a large set of experimentally determined structures and optimized using standard sets of modeled structures, or decoys. No structure used to train or optimize the function was included among those used to test it. When tested against 29 other published main chain
Scoring functions, such as molecular mechanic forcefields and statistical potentials are fundamentally important tools in protein structure modeling and quality assessment. The performances of a number of publicly available scoring functions are compared with a statistical rigor, with an emphasis on knowledge-based potentials. We explored the effect on accuracy of alternative choices for representing interaction center types and other features of scoring functions, such as using information on solvent accessibility, on torsion angles, accounting for secondary structure preferences and side chain orientation. Partially based on the observations made, we present a novel residue based statistical potential, which employs a shuffled reference state definition and takes into account the mutual orientation of residue side chains. Atom- and residue-level statistical potentials and Linux executables to calculate the energy of a given protein proposed in this work can be downloaded from http
Fatness-associated FTO gene variant increases mortality independent of fatness--in cohorts of Danish men. PLoS One. 2009; 4(2):e4428 ...
A Two-Layer Learning Architecture for Multi-Class Protein Folds Classification: 10.4018/978-1-4666-3604-0.ch041: Classification of protein folds plays a very important role in the protein structure discovery process, especially when traditional sequence alignment methods
RF-Phos, Dukka KC, Random Forest, RF, computational biology, machine learning, hydroxylation site, protein classification, general phosphosite, phosphorylation site prediction, post-translational modification, Protein Structure Prediction, Protein Side Chain Packing, symmetry in protein, multi-domain protein structure prediction, North Carolina A&T State University, RFNR, Feature Extraction, Protein
Bindewald, E., U. Höfer, M. Heiler, J. Hesser, and R. Männer. 1998. Protein Structure Prediction With Combinatorial Optimization. In Third Community Wide Experiment On The Critical Assessment Of Techniques For Protein Structure Prediction, Casp3, 77. Third Community Wide Experiment On The Critical Assessment Of Techniques For Protein Structure Prediction, Casp3 ...
Bindewald, E., U. Höfer, M. Heiler, J. Hesser, and R. Männer. 1998. Protein Structure Prediction With Combinatorial Optimization. In Third Community Wide Experiment On The Critical Assessment Of Techniques For Protein Structure Prediction, Casp3, 77. Third Community Wide Experiment On The Critical Assessment Of Techniques For Protein Structure Prediction, Casp3 ...
Protein-ligand binding site prediction from a 3D protein structure plays a pivotal role in rational drug design and can be helpful in drug side-effects prediction or elucidation of protein function. Embedded within the binding site detection problem is the problem of pocket ranking - how to score and sort candidate pockets so that the best scored predictions correspond to true ligand binding sites. Although there exist multiple pocket detection algorithms, they mostly employ a fairly simple ranking function leading to sub-optimal prediction results. We have developed a new pocket scoring approach (named PRANK) that prioritizes putative pockets according to their probability to bind a ligand. The method first carefully selects pocket points and labels them by physico-chemical characteristics of their local neighborhood. Random Forests classifier is subsequently applied to assign a ligandability score to each of the selected pocket point. The ligandability scores are finally merged into the resulting
TY - GEN. T1 - Efficient algorithms to explore conformation spaces of flexible protein loops. AU - Dhanik, A.. AU - Yao, P.. AU - Marz, N.. AU - Propper, R.. AU - Kou, C.. AU - Liu, Guanfeng. AU - Van Den Bedem, H.. AU - Latombe, J. C.. PY - 2007. Y1 - 2007. N2 - Two efficient and complementary sampling algorithms are presented to explore the space of closed clash-free conformations of a flexible protein loop. The seed sampling algorithm samples conformations broadly distributed over this space, while the deformation sampling algorithm uses these conformations as starting points to explore more finely selected regions of the space. Computational results are shown for loops ranging from 5 to 25 residues. The algorithms are implemented in a toolkit, LoopTK, available at https://simtk.org/home/looptk.. AB - Two efficient and complementary sampling algorithms are presented to explore the space of closed clash-free conformations of a flexible protein loop. The seed sampling algorithm samples ...
The protein structure prediction (PSP) problem is concerned with the prediction of native tertiary structure of a protein given its sequence of amino acids. Ab-initio approach to PSP problem assumes that native conformation of protein corresponds to the global minimum free energy state. The potential energy used to evaluate the conformation of a protein is based on different interaction energies. In the present work, potential energy function Chemistry at HARvard Macromolecular Mechanics (CHARMM) has been used to qualitatively assess the conformations. Backbone and side-chain torsion angles are used to represent each conformation. In the present thesis, we have used Bacterial Foraging Optimization Algorithm as a search procedure for exploring the conformational space of the PSP problem. Results obtained indicate that this is another promising way of finding the stable structure of protein ...
Membrane protein characterization at atomic resolution is always a big challenge in development of membrane protein-based antibody as well as small molecule drugs. The development of these membrane protein related antibodies and vaccines require high resolution structural information of target protein. Thus membrane protein characterization plays a vital role in drug discovery, propelling the demand for membrane protein characterization Service across the world. In order to derive atomic models for membrane proteins composing over 50% of overall drug targets, solution-state NMR and X-ray crystallography have been widely used. Membrane protein characterization offer high benefits. Both the solution-state NMR and X-ray crystallography methods have their own drawbacks. However, there exists another method called transmission electron microscopy that is gaining ever-increasing popularity in membrane protein characterization at atomic resolution. Thus reported to be one of the best membrane protein ...
MODBASE (http://guitar.rockefeller.edu/modbase) is a relational database of annotated comparative protein structure models for all available protein sequences matched to at least one known protein structure. The models are calculated by MODPIPE, an automated modeling pipeline that relies on PSI-BLAS …
BACKGROUND: Protein fold recognition usually relies on a statistical model of each fold; each model is constructed from an ensemble of natural sequences belonging to that fold. A complementary strategy may be to employ sequence ensembles produced by computational protein design. Designed sequences can be more diverse than natural sequences, possibly avoiding some limitations of experimental databases. METHODOLOGY/PRINCIPAL FINDINGS: WE EXPLORE THIS STRATEGY FOR FOUR SCOP FAMILIES: Small Kunitz-type inhibitors (SKIs), Interleukin-8 chemokines, PDZ domains, and large Caspase catalytic subunits, represented by 43 structures. An automated procedure is used to redesign the 43 proteins. We use the experimental backbones as fixed templates in the folded state and a molecular mechanics model to compute the interaction energies between sidechain and backbone groups. Calculations are done with the Proteins@Home volunteer computing platform. A heuristic algorithm is used to scan the sequence and conformational
The solvent accessibility of a residue in a protein is a value that represents the solvent exposed surface area of this residue. It is crucial for understanding protein structure and function. As a result of the completion of whole-genome sequencing projects, the sequence-structure gap is rapidly increasing. Importantly, the knowledge of protein structures is a foundation for understanding the mechanism of diseases of living organisms and facilitating discovery of new drugs. The most reliable methods for identification of protein structure are X-ray crystallography techniques, but they are expensive and time-consuming. This leads to a central, yet unsolved study of protein structure prediction in bioinformatics, especially for sequences which do not have a significant sequence similarity with known structures [1]. To predict protein structure, the role of solvent accessibility has been extensively investigated as it is related to the spatial arrangement and packing of amino acids during the ...
DNASTAR NovaFold is protein structure prediction software that is based on I-Tasser, the award-winning software package developed by Prof. Yang Zhangs laboratory at the University of Michigan. NovaFold utilizes the I-Tasser algorithms developed by Prof. Zhang that combine threading and ab initio folding technologies to build accurate, full 3D atomic models of proteins with previously unknown structures.
We introduce a new type of knowledge-based potentials for protein structure prediction, called evolutionary potentials, which are derived using a single experimental protein structure and all three-dimensional models of its homologous sequences. The new potentials have been benchmarked against other knowledge-based potentials, resulting in a significant increase in accuracy for model assessment. In contrast to standard knowledge-based potentials, we propose that evolutionary potentials capture key determinants of thermodynamic stability and specific sequence constraints required for fast folding.
TY - JOUR. T1 - Fatness-Associated FTO Gene Variant Increases Mortality Independent of Fatness - in Cohorts of Danish Men. AU - Zimmermann, E. AU - Kring, SI. AU - Berentzen, TL. AU - Holst, C. AU - Pers, Tune Hannes. AU - Hansen, T. AU - Pedersen, O. AU - Sørensen, TI. AU - Jess, T. N1 - This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.. PY - 2009. Y1 - 2009. N2 - The A-allele of the single nucleotide polymorphism (SNP), rs9939609, in the FTO gene is associated with increased fatness. We hypothesized that the SNP is associated with morbidity and mortality through the effect on fatness. METHODOLOGY/PRINCIPAL FINDINGS: In a population of 362,200 Danish young men, examined for military service between 1943 and 1977, all obese (BMI,or=31.0 kg/m(2)) and a random 1% sample of the others were identified. In 1992-94, ...
Protein interaction networks have become a tool to study biological processes, either for predicting molecular functions or for designing proper new drugs to regulate the main biological interactions. Furthermore, such networks are known to be organized in sub-networks of proteins contributing to the same cellular function. However, the protein function prediction is not accurate and each protein has traditionally been assigned to only one function by the network formalism. By considering the network of the physical interactions between proteins of the yeast together with a manual and single functional classification scheme, we introduce a method able to reveal important information on protein function, at both micro- and macro-scale. In particular, the inspection of the properties of oscillatory dynamics on top of the protein interaction network leads to the identification of misclassification problems in protein function assignments, as well as to unveil correct identification of protein functions. We
Protein structure mining using a structural alphabet.: Protein structure mining using a structural alphabet. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
A novel method, Multiple Mapping Method with Multiple Templates (M4T) is introduced that implements an algorithm to automatically select and combine Multiple Template structures (MT) and an alignment optimization protocol (Multiple Mapping Method, MMM). The MT module of M4T selects and combines mult …
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DNA-binding pseudobarrel domain superfamily domain assignments in TargetDB . Domain assignment details for each protein include region, Evalue and model. Alignments, domain architectures and domain combinations are provided for each group of proteins.
Several novel techniques are employed for protein tertiary structure prediction, but the more successful ones are those that rely either solely or partly on template/homology based modeling of full or sub-structures. However, a critical look at the yearly
Background: Techniques for inferring the functions of the protein by comparing their shape similarity have been receiving a lot of attention. Proteins are functional units and their shape flexibility occupies an essential role in various biological processes. Several shape descriptors have demonstrated the capability of protein shape comparison by treating them as rigid bodies. But this may give rise to an incorrect comparison of flexible protein shapes. Results: We introduce an efficient approach for comparing flexible protein shapes by adapting a local diameter (LD) descriptor. The LD descriptor, developed recently to handle skeleton based shape deformations [1], is adapted in this work to capture the invariant properties of shape deformations caused by the motion of the protein backbone. Every sampled point on the protein surface is assigned a value measuring the diameter of the 3D shape in the neighborhood of that point. The LD descriptor is built in the form of a one dimensional histogram ...
Our focus is the characterization of protein structure, dynamics and interactions, using both solution and solid-state NMR spectroscopy. In the past, we have committed ourselves to the development of innovative NMR methodology as well as application of new and established methods to better understand the behavior of various proteins. In particular, we have a major record in proton-detected solid-state NMR, which is currently transforming into a new state of the art in solid-state NMR. Our interests nowadays are structure and dynamics playing a role for enzymatic function and for protein-small molecule interactions. Our lab has its own new 800 and 700 MHz magnets used for both, solids and solution. We own a broad selection of solids probes, including 3.2, 2.5, 1.3, and 0.7 mm, reaching up to the highest spin rates of commercially available technology above 110 kHz MAS. The biochemistry lab structure is very well set up (including for example a brand-new Beckman Coulter centrifuge and two ÄKTA ...
Chloride channel accessory 1 is a protein that in humans is encoded by the CLCA1 gene. This gene encodes a member of the calcium sensitive chloride conductance protein family. To date, all members of this gene family map to the same region on chromosome 1p31-p22 and share a high degree of homology in size, sequence, and predicted structure, but differ significantly in their tissue distributions. The encoded protein is expressed as a precursor protein that is processed into two cell-surface-associated subunits, although the site at which the precursor is cleaved has not been precisely determined. The encoded protein may be involved in mediating calcium-activated chloride conductance in the intestine. Protein structure prediction methods suggest the N-terminal region of CLCA1 protein is a zinc metalloprotease. Chloride channel GRCh38: Ensembl release 89: ENSG00000016490 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000028255 - Ensembl, May 2017 Human PubMed Reference:. Mouse PubMed ...
Kernel regression or classification (also referred to as weighted $\epsilon$-NN methods in Machine Learning) are appealing for their simplicity and therefore ubiquitous in data analysis. However, practical implementations of kernel regression or classification consist of quantizing or sub- sampling data for improving time efficiency, often at the cost of prediction quality. While such tradeoffs are necessary in practice, their statistical implications are generally not well understood, hence practical implementations come with few performance guarantees. In particular, it is unclear whether it is possible to maintain the statistical accuracy of kernel prediction---crucial in some applications---while improving prediction time.. The present work provides guiding principles for combining kernel prediction with data- quantization so as to guarantee good tradeoffs between prediction time and accuracy, and in particular so as to approximately maintain the good accuracy of vanilla kernel ...
Protein Therapeutics market report takes stock of the global market on the basis of its attractiveness as well as investment viability. It also offers quantitative and qualitative analysis of every feature of the market and catches the emerging industry trends. The aim of the report is to allow the readers to concentrate on the classifications on the basis of product qualifications, standing competitive landscape and the markets incomes with profitability.. The report aims to provide an overview of global market with detailed market segmentation by product, application, end user and geography. The global Protein Therapeutics market is expected to witness high growth during the forecast period. The report provides key statistics on the market status of the leading Protein Therapeutics market players and offers key trends and opportunities in the market.. Get Sample Copy of the [email protected] https://www.theinsightpartners.com/sample/TIPRE00002856/. North America held the dominant share in ...
Protein Science, the flagship journal of The Protein Society, serves an international forum for publishing original reports on all scientific aspects of protein molecules. The Journal publishes papers by leading scientists from all over the world that report on advances in the understanding of proteins in the broadest sense. Protein Science aims...
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Protein folding is a technique through which a protein constitution assumes its useful form of conformation, and has been the topic of study because the book of the 1st software program software for protein constitution prediction. Protein folding in silico techniques this factor via introducing an ab initio version that makes an attempt to simulate so far as attainable the folding strategy because it occurs in vivo, and makes an attempt to build a mechanistic version at the foundation of the predictions made. the outlet chapters speak about the early level intermediate and overdue level intermediate types, by way of a dialogue of structural details that is affecting the translation of the folding technique. the second one half the publication covers numerous issues together with ligand binding web site reputation, the fuzzy oil drop version and its use in simulation of the polypeptide chain, and misfolded proteins. The booklet ends with an outline of a few different ab initio equipment for ...
The YRC PDR provides for the searching of millions of protein descriptions from many databases to find proteins and public experimental data describing those proteins produced by the YRC. The experimental data is in the form of mass spectrometry, yeast two-hybrid, protein structure prediction, light microscopy and protein complex predictions.
The YRC PDR provides for the searching of millions of protein descriptions from many databases to find proteins and public experimental data describing those proteins produced by the YRC. The experimental data is in the form of mass spectrometry, yeast two-hybrid, protein structure prediction, light microscopy and protein complex predictions.
Non-steric-zipper models for pathogenic α-synuclein conformers. May 10, 2019 Related ArticlesNon-steric-zipper models for pathogenic α-synuclein conformers. APL Bioeng. 2018 Jun;2(2):026105 Authors: Schuman B, Won A, Brand-Arzamendi K, Koprich JB, Wen XY, Howson PA, Brotchie JM, Yip CM Abstract Parkinsons disease neurodegenerative brain tissue exhibits two biophysically distinct α-synuclein fiber isoforms-single stranded fibers that appear to be steric-zippers and double-stranded fibers with an undetermined structure. Herein, we describe a β-helical… ...
Protein domains are compact regions of a proteins structure that often convey some distinct function. Domain architecture, or order of domains in a protein, is frequently considered as a fundamental level of protein functional complexity [1]. The majority of the protein repertoire is composed of multidomain proteins; two-thirds of the proteins in prokaryotes and about four-fifths eukaryotic ones have two or more domains [2]. Moreover, an organisms complexity relates much better to the number of distinct domain architectures [3] and expansion in particular domain families [4] than to the number of genes in the organism. The prevalence of proteins with more than two domains and the recurrent appearance of the same domain in non-homologues proteins show that functional domains are reused when creating new proteins. Because of this, domains have been likened to Lego bricks that can be recombined in various ways to build proteins with completely new functions [5]. Hence, one way to study evolution ...
MedAI, provides customers with professional prediction of protein-protein interaction solutions according to their detailed requirements.
Histidine-rich glycoprotein (HRG)is a glycoprotein that in humans is encoded by the HRG gene. The HRG protein is produced in the liver, and it could also be synthesized by monocytes, macrophages, and megakaryocytes. It possesses a multi-domain structure, which makes it capable of binding to numerous ligands and modulating various biological processes including immunity, vascularization and coagulation. The HRG gene lies on location of 3q27 on the chromosome 3, spans approximately 11kb, and consist of 7 exons. Two common isoforms of the HRG gene have been found in humans. These isoforms exist due to a polymorphism occurring in exon 5. HRG is a glycoprotein of 70-75kDa present at a relatively high concentration in the plasma of vertebrates. The primary structure of human HRG is predicted to be a 507 amino acid multidomain polypeptide consisting of two cystatin-like regions at the N-terminus, a histidine-rich region (HRR) flanked by proline-rich regions (PRR), and a C-terminal domain. HRG has an ...
As a remarkable pioneer in the field of studying protein-protein interactions (PPIs), Profacgen provides a novel technique, proximity-dependent biotin identification (BioID), which has been used for identification of proteins in the close vicinity of a protein of interest in living cells.. The introduction of BioID. Determining protein partners is an essential step toward understanding protein function and identifying relevant biological pathways. However, many conventional methods for investigating protein-protein interactions can be merely used in vitro, which may not reflect the actual interaction in native environments, or often encounter the loss of candidate proteins because of transient or weak protein interactions or protein insolubility.. BioID has emerged as a new tool based on enzyme-catalyzed proximity labeling (PL), to provide the possibility to study the spatial and interaction characteristics of proteins in living cells (Roux et al., 2012). Its main principle is that utilize the ...
Predicting the function of an uncharacterized protein is a major challenge in post-genomic era due to problems complexity and scale. Having knowledge of protein function is a crucial link in the...
Motivation:In silico methods are being widely used for identifying substrates for various kinases and deciphering cell signaling networks. However, most of the available phosphorylation site prediction methods use motifs or profiles derived from a known data set of kinase substrates and hence, their applicability is limited to only those kinase families for which experimental substrate data is available. This prompted us to develop a novel multi-scale structure-based approach which does not require training using experimental substrate data.. Results:In this work, for the first time, we have used residue-based statistical pair potentials for scoring the binding energy of various substrate peptides in complex with kinases. Extensive benchmarking on Phospho.ELM data set indicate that our method outperforms other structure-based methods and has a prediction accuracy comparable to available sequence-based methods. We also demonstrate that the rank of the true substrate can be further improved, if ...
Scientists have solved 1,000 protein structures using data collected at CLSs CMCF beamlines. These have been added to the Protein Data Bank - a collection of structures solved by researchers globally.
Howto figure out whether two lists have any elements in common - While working with FragIt I had to figure out whether two lists had some elements in common (it does not matter which!) and I came up with the following pi... ...
Get the same high-quality protein shakes, diet shakes and weight loss shakes used by physicians and weight loss clinics, delivered to your door at discount prices.You have landed on a site that is sure to help you make a smarter decision about choosing the right meal replacement.There are now 105 different protein shake recipes in our list - for muscle gain, fat loss, energy, and some just for fun.Get the same high-quality protein diet shakes used by physicians and weight loss centers quickly and efficiently delivered to your door.. Meal-replacement shakes are an effective, easy way to drop pounds ...
You will need extra protein. This is because some protein is lost into the peritoneal fluid. If you do not eat enough protein, dialysis can cause protein deficiency and muscle loss. Your dietitian will help determine how much protein you need. Make sure that the protein you eat is high-quality. High-quality protein sources include meat, fish, poultry, and eggs. Milk contains high-quality protein, but it is also high in potassium and phosphorous. Grains and vegetables contain low-quality protein. You may need to limit your intake of these. ...
The Protein Data Bank hosts the current body of structural data on proteins and their complexes that has been acquired so far by researchers from all over the world. Beyond that, under General Education it also offers the Molecule of the Month: concise but at the same time thrilling accounts on selected molecules to be found in the Protein Data Bank. The stories are presented by David S. Goodsell, together with beautifully painted images of the protein structures. To the right you can see a reproduction of Goodsells painting of the Cholera Toxin. Such pore-proteins have inspired some of our research on DNA origami nanopores. If you ever wondered why some bacteria make you sick, read this shocking story about Cholera (original story and how it relates to other bacterial toxins to be found here): Cholera Toxin Sept 2005 Molecule of the Month by David S. Goodsell Bacteria pull no punches when they fight to protect themselves. Some bacteria build toxins so powerful that a single molecule can ...
Protein microarrays provide an efficient method to recognize and quantify protein-protein connections in great throughput. will end up being described at length in the protocols beneath. Measuring binding affinities acts at least three reasons. First the excess rigor necessary to quantify connections minimizes the quantity of wrong details in the ultimate NVP-BAG956 data set. Many high-throughput methods have got alarmingly high prices of fake positives and fake negatives22-25 restricting their effectiveness in generating natural hypotheses. Second identifying binding affinities really helps to prioritize which connections will end up being biologically relevant. Finally quantitative information pays to for modeling studies targeted at predicting protein-protein interactions especially. Furthermore to offering binding affinities proteins microarrays also enable someone to assess how well a ligand is normally acknowledged by every person in a proteins family. As such they offer details on binding ...
Understanding the 3D molecular structure of proteins is of enormous importance in science, medicine and biotechnology. When determining the 3D structure of a protein using biophysical methods, it is often assumed that a protein molecule has a single, specific shape. Yet in reality, many proteins adopt a number of radically different conformations, that can interchange dynamically. Such a set of conformations is called an ensemble. It is precisely the ensemble aspect of protein structure that plays a major role in important diseases such as Parkinsons, type II diabetes or Alzheimers. Currently, there are few methods that can handle such ensembles, and the available methods are suboptimal, ad hoc and heuristic.. We have developed a statistically rigorous and computationally efficient method to determine the structure of protein ensembles (Olsson et al., J. Magn. Reson., 2010; Olsson et al., PLoS ONE, 2013), based on previous methods developed at the Bioinformatics center, targeting both NMR and ...
The study of protein evolution is complicated by the vast size of protein sequence space, the huge number of possible protein folds, and the extraordinary complexity of the causal relationships between protein sequence, structure, and function. Much simpler model constructs may therefore provide an attractive complement to experimental studies in this area. Lattice models, which have long been useful in studies of protein folding, have found increasing use here. However, while these models incorporate actual sequences and structures (albeit non-biological ones), they incorporate no actual functions-relying instead on largely arbitrary structural criteria as a proxy for function. In view of the central importance of function to evolution, and the impossibility of incorporating real functional constraints without real function, it is important that protein-like models be developed around real structure-function relationships. Here we describe such a model and introduce open-source software that implements
TY - JOUR. T1 - Histidine-rich glycoprotein prevents septic lethality through neutrophil regulation. AU - Nishibori, M.. AU - Wake, H.. AU - Mori, S.. AU - Liu, K.. AU - Morioka, Y.. AU - Teshigawara, K.. AU - Sakaguchi, M.. AU - Kuroda, K.. AU - Takahashi, H.. AU - Ohtsuka, A.. AU - Yoshino, T.. AU - Morimatsu, H.. PY - 2014/12/3. Y1 - 2014/12/3. UR - http://www.scopus.com/inward/record.url?scp=84928530987&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=84928530987&partnerID=8YFLogxK. U2 - 10.1186/cc14026. DO - 10.1186/cc14026. M3 - Article. AN - SCOPUS:84928530987. VL - 18. SP - 1. EP - 53. JO - Critical Care. JF - Critical Care. SN - 1466-609X. IS - 2. ER - ...
Constraints and Molecular Biology: Constraint Programming techniques can be efficiently used for predicting structure of a protein which is considered one of the most important problem in Computational Biology. The protein structure prediction problem has effectively been transformed to a constraint minimization problem with finite domain and Boolean variables. The Oz language was then used to implement the constraint problem. Certain variables have been defined for the entire constraint problem of predicting the protein structure. Later constraint optimization has been used to minimize the variable surface. A perfect conformation was found on all possible sequences in finding the sequence length and also the optimal surface. Hence constraint techniques can be effectively applied to solving problems in computational biology.. Read More ...