Biophysical properties conformational protein protein proteins magnetic resonance spectroscopy. Medical search. Frequent questions

In this chapter, we describe the use of high-pressure coupled to Nuclear Magnetic Resonance (NMR) spectroscopy to reveal unprecedented details on the folding energy landscape of proteins. (pasteur.fr)
In order to better understand the complex formation of GAP-43 and BASP1, nuclear magnetic resonance (NMR) spectroscopy in combination with other biophysical methods are employed for this work. (univie.ac.at)
Our lab studies the structure and dynamics of proteins, protein-protein complexes, and protein-nucleic acid complexes using multidimensional nuclear magnetic resonance (NMR) spectroscopy, and we develop and apply novel NMR and computational methods to aid in these studies. (nih.gov)
Our studies rely on nuclear magnetic resonance (NMR) spectroscopy, a research approach that relies on the magnetic properties of the nucleus of certain atoms to determine physical and chemical properties of the molecules in which they are contained. (nih.gov)
An overview of the metabolic differences between Bradyrhizobium japonicum 110 bacteria and differentiated bacteroids from soybean (Glycine max) root nodules : an in vitro C- and P-nuclear magnetic resonance spectroscopy study. (ibs.fr)
Nuclear Magnetic Resonance ( NMR ) spectroscopy is a powerful tool for the study of structural biology, structure/activity relationships and macromolecule and small-molecule analysis. (irbm.com)
Our principal experimental tool is nuclear magnetic resonance (NMR), in particular nuclear spin relaxation measurements. (lu.se)
Nuclear magnetic resonance spectroscopy, Radiolabeling, Biomolecules-Analysis, Isotope Labeling-methods, Nuclear Magnetic Resonance, Biomolecular Here we describe a protocol for the labeling of proteins that facilitates their study using a technique that is sensitive to millisecond conformational exchange restrict to techniques of labeling with isotopes (stable or radioactive): do not use for radioisotope tracer studies of "labeled" cells, microorganisms or chemicals Pris: 1862 kr. (firebaseapp.com)
Commonly, micelles (spherical aggregates formed by short-chain lipids above a critical micelle concentration) or bicelles (discoidal aggregates formed by mixing short- and long-chained lipids) solubilise and stabilise membrane proteins for crystallisation and solution state Nuclear Magnetic Resonance (NMR) analysis. (mappingignorance.org)
X-ray crystallography and nuclear magnetic resonance (NMR) are usually employed to determine the structure of peptides [15] -[17] , but while these analytical methods are excellent for three-dimensional structural determination at the atomic level, they are also time consuming, and once analyzed, samples cannot be re-used for other analytical methods. (scirp.org)
Although high-resolution structural information can be obtained by X-ray crystallography, cryo-electron microscopy, nuclear magnetic resonance, and structure prediction tools, they are often insufficient for grasping the actual states of proteins in solution. (biophysics.org)

Such states, which are invisible to conventional biophysical techniques, including crystallography, play a critical role in macromolecular recognition, allostery induced fit, conformational selection, and molecular assembly. (nih.gov)
They might first use NMR or surface plasmon resonance to screen and then X-ray crystallography to determine the structure of the fragment-protein complex. (the-scientist.com)
We also collaborate with other groups for Mossbauer, electron-nuclear double resonance (ENDOR), X-ray absorption and X-ray crystallography studies of proteins prepared in our laboratory. (uga.edu)
The known membrane protein structures, derived mainly by crystallography, provide little insight into lipid-protein interactions as bound lipid molecules are rarely visible. (mappingignorance.org)

This conformational change exposes a large hydrophobic pocket between helix 3, 4, and the hinge region of S100A1 that is involved in virtually all calcium-dependent target protein interactions. (wikipedia.org)
Exploration of the supramolecular interactions involving tris-dipicolinate lanthanide complexes in protein crystals by a combined biostructural, computational and NMR study. (ibs.fr)
We have a set of biophysical tools available that allow, for example, the determination of binding kinetics , affinity and specificity , secondary structure and thermodynamic profiles, or structural insights on the molecular interactions of a small molecule or a peptide to its target. (irbm.com)
To support our discovery programs we can use CD spectroscopy for different applications for the study of secondary structure content of peptides and proteins, monitoring conformational transitions , and the study of the thermodynamics of unfolding and protein-ligand interactions . (irbm.com)
The fast and real time analysis of the kinetic and thermodynamic binding parameters of small molecules , peptides , antibodies , or other protein-protein interactions, are crucial information for target characterization, hit identification, lead optimization or characterization of the binding properties of a molecule to its target. (irbm.com)
As the assembly was carried out in the absence of ATP, this suggests that formation of the holoenzyme from the individual subcomplexes is solely driven by protein-protein interactions at the interface. (upstate.edu)
Unlike reversible disassembly, which requires ATP hydrolysis on V 1 to break protein-protein interactions, Oxr1p mediated disassembly of V-ATPase is ATP independent and therefore a novel mode of activity regulation. (upstate.edu)
Impact of nucleic acid self-alignment in a strong magnetic field on the interpretation of indirect spin-spin interactions. (muni.cz)
molecular-level understanding of the structure, stability, interactions and dynamics of proteins. (lth.se)
describe the principal physico-chemical properties of proteins, such as structure, stability, interactions and dynamics. (lth.se)
Analysis of structure, interactions and dynamics of proteins in solution. (lth.se)
Molecular interactions in cell membranes, particularly lipid-protein interactions in their hydrophobic core, are difficult to analyse and remain poorly characterised despite high relevance in physiological and pathological processes. (mappingignorance.org)
Structural rearrangements in membranes and embedded proteins, and the way molecular interactions contribute to their function are unresolved questions in biophysical chemistry. (mappingignorance.org)
Our new article 1 present the proof of concept of a generalized approach for NMR studies of lipid-protein interactions that relies on sparse fluorination of the lipid acyl chains and exploits fluorine both indirectly, as shift reagent affecting the NMR signals of nearby atoms, and directly, as 19 F isotope with unique NMR properties. (mappingignorance.org)
Protein-protein interactions involving intrinsically disordered proteins are important for cellular function and common in all organisms. (elifesciences.org)
Experiments together with molecular modeling using NMR chemical shifts suggest that new interactions involving intrinsically disordered proteins may evolve via a low-affinity complex which is optimized by modulating direct interactions as well as dynamics, while tolerating several potentially disruptive mutations. (elifesciences.org)
At multiple time points during evolution, new or modified proteins - and consequently new potential interactions between proteins - have emerged. (elifesciences.org)
The findings shed light on fundamental principles of how new protein-protein interactions emerge and evolve on a molecular level. (elifesciences.org)
A next step for the future will be to investigate how other protein-protein interactions have evolved and to identify general underlying patterns. (elifesciences.org)
A deeper knowledge of how this molecular evolution happened will broaden our understanding of present day protein-protein interactions and might aid the design of drugs that can mimick proteins. (elifesciences.org)
Theoretically a radical pair could be described though the Hamilton operator that includes interactions between unpaired electrons and nuclei, the so-called hyperfine interactions, as well as the Zeeman interaction between the magnetic field and the electrons. (nature.com)
Due to those interactions, the magnetic field influences the total spin character of the radical pair, continuously altering it between the triplet and the singlet states. (nature.com)
FLIM-FRET analysis of protein-protein interactions showed that PLIN5 S155 phosphorylation regulates PLIN5 interaction with adipose triglyceride lipase at the lipid droplet, but not with α-β hydrolase domain-containing 5. (uci.edu)
Protein complexes, which are formed as a result of these interactions, consist of two or more components that associate along specific pathways - protein association pathways. (lu.se)
The MIPs are produced by various polymerization methods but in all cases specifi c interactions, molecular partitioning and polymer structure are key properties that we focus on. (lu.se)
Chemical structures of the interfaces along with the electrical, mechanical and morphological properties at nanoscale appear equally relevant to drive the interactions between living and synthetic systems. (european-mrs.com)

Defining the physical-chemical determinants of protein folding and stability, under normal and pathological conditions has constituted a major subfield in biophysical chemistry for over 50 years. (pasteur.fr)
Prizes and awards include the Royal Society of Chemistry Centenary and Khorana Prizes, the Biochemical Society (U.K.) Centenary Award, The Biophysical Society Innovation Award, and the Biopolymers Murray Goodman Memorial Prize. (nih.gov)
To use this technique in your laboratory, you'll need access to a team with a diverse set of skills: structural biology, organic synthesis and medicinal chemistry, biophysical assays, and even chemical informatics and molecular modeling. (the-scientist.com)
The research activities within the Division fall mostly within the broad, interdisciplinary field of biophysical chemistry. (lu.se)
The course literature consists of the compendium "Biophysical Chemistry", authored and updated each year by the course teachers, and of manuals for the practicals. (lth.se)

Isotope Labeling Biophysical Techniques for Structural Characterization of Macromolecules. (firebaseapp.com)
Protein characterization by optical spectroscopy: Physical principles and applications of fluorescence and circular dichroism spectroscopy. (lth.se)
We performed phylogenetic reconstruction, resurrection and biophysical characterization of two interacting disordered protein domains, CID and NCBD. (elifesciences.org)

These include characterizing the structural, thermodynamic and dynamic properties of the barriers between conformational states on the protein energy landscape, understanding the sequence dependence of folding cooperativity, defining more clearly the role of solvation in controlling protein stability and dynamics and probing the high energy thermodynamic states in the native state basin and their role in misfolding and aggregation. (pasteur.fr)
The purpose of my lab's research is to understand the interrelationship between the structure, dynamics, and function of proteins. (nih.gov)
Our lab is developing new tools and techniques that facilitate the study of the structure and dynamics of proteins and protein complexes, functional units that include one or more proteins. (nih.gov)
Change of dynamics of raft-model membrane induced by amyloid-beta protein binding. (ibs.fr)
The ecology of protein dynamics. (ibs.fr)
This includes gene, protein and metabolic networks, cellular architecture and intracellular dynamics, cell communication and motility, cell division and differentiation, tissue formation and organogenesis, tissue and organ functions, changes in population characteristics as a consequence of interaction of organisms with their physical environment, with individuals of their own species, and with organisms of other species. (nih.gov)
Experimental methods of multi-dimensional NMR spectroscopy, dynamics and theoretical description of spin system evolution, multiple resonance NMR technique for structural studies of proteins and nucleic acids by NMR spectroscopy, contemporary methods of structural biology, studies of complex biomolecular systems. (muni.cz)
Articles, abstracts, and book chapters citing Globals Software (Globals Unlimited, Globals for Spectroscopy, and Globals for Images aka SimFCS) by authors not affiliated with the Laboratory for Fluorescence Dynamics (LFD). (uci.edu)
A higher magnitude of conformational dynamics and variations are expected, especially for multi-domain proteins consisting of multiple structural domains. (biophysics.org)
The trajectory of the inter-gadolinium distance as predicted by molecular dynamics (MD) simulation is shown at the bottom, depicting drastic conformational changes of MurD. (biophysics.org)
We also investigated the conformational dynamics of the same protein by X-ray scattering, neutron scattering, and MD simulation. (biophysics.org)
Quasielastic incoherent neutron scattering (QENS) is a well-suited experimental method to study protein dynamics from the picosecond to several nanoseconds and in the Ångström length-scale. (lu.se)
In my presentation, I will summarize recent QENS and NSE results on the dynamics of the intrinsically disordered myelin basic protein (MBP) and the chemically denatured bovine serum albumin (BSA) (1,2,3). (lu.se)

interpret experimental results from physico-chemical studies of proteins. (lth.se)

A particular focus is the study of rare, highly transient, "excited" states of proteins and their complexes that play a key role of molecular recognition. (nih.gov)
We are particularly interested in complexes involved in signal transduction and transcriptional regulation, and on AIDS and AIDS-related proteins. (nih.gov)
The many proteins and protein complexes we describe are resulting in new insights into fundamental cell operations. (nih.gov)
New technologies for purifying membrane-bound protein complexes in combination with cryo-electron microscopy (EM) have recently allowed the exploration of such complexes under near-native conditions. (researchgate.net)

Highly divergent hypotheses have been put forward regarding the makeup of the prions, including that they consist of nucleic acid only or protein only, are lacking both protein and nucleic acid, or are a polysaccharide. (medscape.com)
Changes in the redox state of cells affect proteins, lipids, and nucleic acids in different ways. (hindawi.com)
Peptides and nucleic acids can self-assemble to give supramolecular structures that find application in different fields, ranging from the delivery of drugs to the obtainment of materials endowed with optical properties. (cnr.it)

74] V. Chevelkov, K. Giller, S. Becker, and A. Lange, Measurement of backbone hydrogen-deuterium exchange in the type III secretion system needle protein PrgI by solid-state NMR, Journal of Magnetic Resonance , 283 (2017), pp. 110-116. (leibniz-fmp.de)

CD is a powerful tool for studying peptide and protein conformation requiring a minimal amount of sample compared to other techniques. (irbm.com)
After obtaining his degree in 1997, he worked as a Wellcome Trust and BBSRC Research Fellow, designing joint theoretical and experimental approaches to study the dynamic conformation of hyaluronan, both free and in the presence of protein, and expanding his research into other polysaccharides and oligosaccharides. (gr.jp)
The infectious agent in the prion disease is composed mainly or entirely of an abnormal conformation of a host-encoded glycoprotein called the prion protein. (medscape.com)
The replication of prions involves the recruitment of the normally expressed prion protein, which has mainly an alpha-helical structure, into a disease-specific conformation that is rich in beta-sheet. (medscape.com)

The reason why Peter Lansbury and others used the term 'natively unfolded' for a-synuclein and other proteins, especially peptides, is that they do not exist, to a significant degree, in the same kind of stable structure that larger native proteins like myoglobin do. (alzforum.org)

The Applications in human mineral Isotopic labeling of compounds is a non-radioactive method of labeling, provides site-specific investigation of structures, makes molecules easily detectable by mass spectrometry and NMR, maintaining the physico-chemical properties of the target molecule, and is cost-effective and easy to use. (firebaseapp.com)

For the September 2023 issue, we are highlighting Alexandra Ros, an associate editor for Biophysical Reports . (biophysics.org)

Biophysical assays are the ideal photon-based assay companion. (irbm.com)
Specific protein-binding measures are often used as assays in diagnostic assessments. (lookformedical.com)

account for these properties in terms of molecular-level theroetical models. (lth.se)
Moreover, a molecular-level understanding of iron-sulfur cluster biogenesis is crucial for understanding a variety of human diseases involving anemias, myopathies and ataxias that arise from defects in Fe-S cluster biogenesis proteins. (uga.edu)
Research on Fe-S cluster biosynthesis in the Johnson group currently involves investigating the molecular mechanisms of Fe-S cluster assembly on scaffold proteins and the subsequent intact cluster transfer to acceptor or carrier proteins. (uga.edu)
NMR spectroscopy, contrarily, does not require molecular order and lipid-protein contacts may be sampled at low resolution to gauge protein insertion into the lipid layer, e.g. by use of paramagnetic agents that perturb the NMR signals of nearby membrane protein atoms. (mappingignorance.org)
The classic workaround to correlate 1 H with the better resolved 13 C frequencies is impractical for lipids where the required 13 C isotope enrichment is costly, may not resolve all overlap problems, and provides no distinct molecular marker from a likewise 13 C labelled protein to single out inter- from intramolecular NOE signals. (mappingignorance.org)
at the same time developing protein and peptide-based tools that will allow us to manipulate cellular processes on a molecular level. (stanford.edu)
Alpha-crystallins also act as molecular chaperones that bind to denatured proteins, keep them in solution and thereby maintain the translucency of the lens. (lookformedical.com)
See also David Thirumalai's Emerging Ideas on the Molecular Basis of Protein and Peptide Aggregation ' (.pdf). (alzforum.org)

The ancestral proteins were then 'resurrected' by recreating them in test tubes and their characteristics and properties analyzed with experimental and computational biophysical methods. (elifesciences.org)
Although HA self-association might provide a possible explanation of some properties of HA, it was important to understand if it is compatible with all the experimental analysis of HA properties. (gr.jp)
Different biophysical, experimental, and computational methods shed light on various aspects of MurD, unveiling the highly dynamic structures of MurD in solution. (biophysics.org)

MARV assembles and buds from the host cell plasma where MARV matrix protein (mVP40) dimers associate with anionic lipids at the plasma membrane inner leaflet and undergo a dynamic and extensive self-oligomerization into the structural matrix layer. (uci.edu)

Many intrinsically disordered proteins have the potential to interact simultaneously or sequentially with a range of different partner molecules. (univie.ac.at)
However, the ability to crystallize or solve an NMR structure of your protein once fragments are bound to it makes it far easier to understand how those molecules bind to a target of interest and to begin to develop those fragments into larger molecules. (the-scientist.com)
HA is polydisperse and its properties are the aggregate properties of a population of molecules of varying chain length, rather than those of a unique species. (gr.jp)
HMGB1 is an abundant protein, 10 6 molecules per cell [ 7 ], which has been postulated as a redox sensor [ 8 ]. (hindawi.com)
He loved microscopes and watching the proteins and molecules that make up cells move around. (biophysics.org)

Small angle neutron scattering for the study of solubilised membrane proteins. (ibs.fr)
In particular, polymer-encapsulated nanodiscs enable the study of membrane proteins at high resolution while retaining protein-protein and protein-lip. (researchgate.net)
For instance, H/F substitution alters the charge distribution in the acyl chain, Also, interaction with membrane proteins may be affected As a drawback for NMR studies, H/F substitution reduces the 1 H density and, thus, coverage of (fluoro)lipid-protein contacts via 1 H, 1 H NOE signals. (mappingignorance.org)

76] M. Zinke, P. Fricke, S. Lange, S. Zinn-Justin, and A. Lange, Protein-protein interfaces probed by methyl-labeling and proton-detected solid-state NMR spectroscopy, ChemPhysChem , 19 (2018), pp. 2457-2460. (leibniz-fmp.de)

carry out spectroscopic measurements on proteins. (lth.se)
In our work we use a range of spectroscopic techniques to probe the characteristic properties of transition metal centers, i.e. color, paramagnetism, etc. (uga.edu)

Much of this early work was based on biophysical measurements of light scattering, osmometry, viscosity and sedimentation and this gave an evolving understanding of non-ideal behaviour and provided a basic structural model for HA that was consistent with results from the different techniques. (gr.jp)
The cover image for the 120/15 issue of Biophysical Journal conceptually shows the investigation of the conformational variation of a multidomain protein, MurD, based on the inter-gadolinium distance measurements. (biophysics.org)
Our study demonstrated that gadolinium tagging of specific positions on the protein enables EPR distance measurements for probing the conformational ensemble of the protein. (biophysics.org)
The distance measurements are coupled with the MD simulation to visualize the structural variations of the protein. (biophysics.org)

These include electron paramagnetic resonance (EPR), resonance Raman, FTIR, and UV/visible/near-IR absorption and natural and magnetically induced circular dichroism (CD and MCD). (uga.edu)
The structural change was determined by using conventional Fourier transform infrared (FTIR) spectroscopy in the previous study. (scirp.org)

Combining small-angle neutron and X-ray scattering for studying protein denaturation. (ibs.fr)
Combining NMR and small angle X-ray and neutron scattering in the structural analysis of a ternary protein-RNA complex. (ibs.fr)
Neutron Spin-Echo spectroscopy (NSE) on the other hand, offers the highest energy resolution in the field of neutron spectroscopy and allows the study of slow collective motions in proteins up to several hundred nanoseconds and in the nanometer length-scale. (lu.se)

A central aspect is then the ability to optimize the functional properties with high spatial resolution, creating materials that are able to control the interaction with the biological surrounding at the nanoscale thus guiding the responses of biomolecules, cells and tissues. (european-mrs.com)

In our study, we exploited a paramagnetic lanthanide ion, Gd 3+ , in electron paramagnetic resonance (EPR) experiments and measured the inter-gadolinium distance distribution that reflects the conformational states of the protein. (biophysics.org)

knowledge about the principal physical methods used in modern protein science. (lth.se)
From its initial isolation, the properties of HA provided a challenge to classical biophysical methods of analysis, which were primarily developed for proteins and required that the properties approached those of perfect Newtonian solutes. (gr.jp)
For biomedical applications, we are combining rational design and combinatorial methods to create designer protein therapeutics and diagnostic agents. (stanford.edu)

Post-Doctoral Researcher, Marie-Curie Fellow (1998-2000), Università degli Studi di Firenze & Center of Magnetic Resonance ( CERM ), Florence, ITALY. (upatras.gr)

Yet, these proteins play important roles in many processes that require the protein to interact with a number of other proteins. (elifesciences.org)

The information content of these techniques is often complementary and leads to a detailed information concerning the electronic, magnetic, and structural properties of metal centers imbedded in a large polypeptide macromolecule. (uga.edu)

Circular dichroism (CD) spectroscopy is a measurement of the difference in absorbance of right and left-circularly polarized light. (irbm.com)
Low-temperature magnetic circular dichroism studies of iron-sulfur proteins. (uga.edu)

Since the rather recent discovery of their crucial role in protein interaction networks intrinsically disordered proteins (IDPs) are subject to intense investigations. (univie.ac.at)

use physico-chemical concepts and models to solve problems involving proteins. (lth.se)

The polymer complex consists of ISCA1 protein monomers with internally bound iron sulphur clusters and simultaneously binds ten cryptochromes. (nature.com)

The latter represents a conformationally modified form of a normal cellular PrP C , which is a normal host protein found on the surface of many cells, in particular neurons. (medscape.com)

We used NMR to determine conformational ensembles of E627 and K627 forms of 627-NLS of PB2 in complex with avian and human ANP32A. (nature.com)
The similar problem is faced when resolving conformational ensembles from small angle scattering data. (lu.se)

These amyloid plaques are immunoreactive with antibodies to the prion protein and do not immunoreact with antibodies to other amyloidogenic proteins, such as the amyloid-beta (which is deposited in Alzheimer disease). (medscape.com)

They are known to bind Calmodulin (by very distinct modes), are substrates of Protein Kinase C and co- localize with phosphatidylinositol-4,5-bisphosphate. (univie.ac.at)
STEP BY STEP: This plan illustrates one set of steps by which researchers can screen for fragments that bind to a protein target of interest. (the-scientist.com)

COURTESY OF RODERICK HUBBARD, J. SYNCHROTRON RAD, 15:227-230, 2008 First you'll need to choose the protein target that you'd like to study. (the-scientist.com)
Synchrotron-radiation infrared microscopy (SR-IRM) is a powerful tool for in situ analysis of minute structural changes of various materials, and in this study, the feasibility of SR-IRM for analyzing the microscopic conformational changes of amyloid fibrils after FEL irradiation was investigated. (scirp.org)

However, a complete understanding of the microscopic shape of HA and how this translates into the macro physical properties has been much more elusive. (gr.jp)

S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. (wikipedia.org)
Fe-S clusters are present in more than 300 different types of enzymes or proteins and play crucial roles in fundamental life processes such as respiration, photosynthesis and nitrogen fixation. (uga.edu)
This review describes recent advances in the role of human HMGB proteins and other proteins interacting with them, in cancerous processes related to oxidative stress, with special reference to ovarian and prostate cancer. (hindawi.com)
Because multi-domain proteins often undergo drastic conformational changes during their functional processes, information about their dynamic properties is essential to understand the mechanisms. (biophysics.org)
The genetic information of life on Earth have been conserved in natural nucleotides-A, G, C, T(U) forming two exclusive sets of base pairs A-T(U) & G-C, that complementing to the fundamental processes of DNA replication & RNA transcription by several polymerases and translation to functional proteins via ribosomal reactions. (fortuneonline.org)

Spectral density mapping at multiple magnetic fields suitable for C-13 NMR relaxation studies. (muni.cz)

This feature enables them to sample an enormous and heterogeneous conformational space. (univie.ac.at)
A heterogeneous family of water-soluble structural proteins found in cells of the vertebrate lens. (lookformedical.com)

The most accurate high-resolution solution structure of human apo-S100A1 protein (PDB accession code: 2L0P) has been determined by means of NMR spectroscopy in 2011. (wikipedia.org)
CD spectra in the far UV range report for secondary structures while in the near UV they are characteristics of the tertiary structure of proteins. (irbm.com)
The biophysical meaning of ccrit remained mostly obscure, since typical low values of ccrit in the sub-µM range hamper investigations of potential oligomeric states and their structure. (researchgate.net)
The specific order of amino acids in a protein determines its shape and structure, which in turn controls what the protein can do. (elifesciences.org)
However, a group of proteins called 'intrinsically disordered proteins' are flexible in their shape and lack a stable three-dimensional structure. (elifesciences.org)
Although the effect of different alcohols on the structure and properties of reverse micelles has been studied for a long time, 232-234 the distribution of alcohols into the water pool or at the interface has only been analyzed in terms of their bulk miscibility properties. (azpdf.net)
Here we describe the 3.2 Å cryo-EM structure of human DEC-205, thereby illuminating the structure of the mannose receptor protein family. (uci.edu)
This result demonstrates that conformational changes of the fibril structure after the FEL irradiation can be observed at a high spatial resolution using SR-IRM analysis and the FEL irradiation system can be useful for dissociation of amyloid aggregates. (scirp.org)
Intrinsically disordered regions (IDRs) lacking a fixed three-dimensional protein structure are widespread and play a central role in cell regulation. (iucr.org)
This would fundamentally change our conventional thinking about protein structure-function relationship, no? (alzforum.org)
I do not think there is a contradiction to the conventional thinking of protein structure-function relation. (alzforum.org)

Stimulated by the pioneering studies on the cationic porphyrin TMPyP4 and the natural product telomestatin, follow-up studies have developed, rapidly leading to a large diversity of macrocyclic structures with remarkable-quadruplex binding properties and biological activities. (hindawi.com)

12. C. This gives a Amino-acid selective isotope labeling of proteins offers numerous advantages in mechanistic studies by revealing structural and functional information unattainable from a crystallographic approach. (firebaseapp.com)
The structural and functional integrity of this overhang is based on its association with a constellation of specific proteins, some of them belonging to the shelterin complex [ 10 ]. (hindawi.com)

The cryo-EM analysis also revealed a population of free V 1 bound to Oxidation Resistance 1 (Oxr1p), a poorly characterized protein that has been implicated in protecting cells from oxidative stress. (upstate.edu)
The results showed that the ancestral proteins created weaker bonds between them compared to more 'modern' ones, and were more flexible even when bound together. (elifesciences.org)
In QENS experiments of protein solutions hydrogens act as reporters for the motions of methyl groups or amino acids to which they are bound. (lu.se)
An interleukin-1 subtype that is synthesized as an inactive membrane-bound pro-protein. (lookformedical.com)

Assessment of ligand binding to the SARS-CoV-2 main protease by saturation transfer difference NMR spectroscopy. (upatras.gr)
The data show that the protein enzyme MurD exists in a wide variety of the conformational states that were eliminated by ligand binding. (biophysics.org)

The characteristic macro physical properties of hyaluronan (HA), which distinguish it from the other components of extracellular matrix, are readily accessible to experimentation and have been investigated and commented upon for over 50 years. (gr.jp)

However, efficient labeling of proteins with selected amino acids necessitates auxotrophic hosts, which are often not available. (firebaseapp.com)

Currently, we are especially interested in developing novel NMR approaches to detect and visualize short-lived, sparsely-populated states that are invisible to conventional biophysical and structural techniques. (nih.gov)

analyzed the amino acid sequences of two specific intrinsically disordered proteins from different organisms to reconstruct the versions of the proteins that were likely found in their common ancestors 450-600 million years ago. (elifesciences.org)

A cell-penetrant peptide blocking C9ORF72-repeat RNA nuclear export reduces the neurotoxic effects of dipeptide repeat proteins. (le.ac.uk)

Metal centers constitute the active sites of at least one third of all enzymes and determining the assembly mechanism of metallocenters and the electronic and structural properties of metal centers that confer selective and specific catalytic activity present fascinating challenges to inorganic chemists. (uga.edu)

Fundamental to the elucidation of these questions is a complete thermodynamic parameterization of protein folding determinants. (pasteur.fr)
Protein Folding and Neurodegeneration: Biophysics to the Rescue? (alzforum.org)
This does not change our view of protein folding in the least. (alzforum.org)

In fact, while they often lack the throughput required for a primary readout (though some recent advances are pushing old boundaries), they allow label-free detection where the measurement directly corresponds to a biophysical variation. (irbm.com)

shown in red), a poorly characterized protein implicated in oxidative stress response. (upstate.edu)

Protein performs its biological functions by interacting with other proteins. (lu.se)

The Heat Stability of Rhamnolipid Containing Egg-Protein Stabilised Oil-In-Water Emulsions. (upatras.gr)

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