TY - JOUR. T1 - Structural genomics target selection for the New York consortium on membrane protein structure. AU - Punta, Marco. AU - Love, James. AU - Handelman, Samuel. AU - Hunt, John F.. AU - Shapiro, Lawrence. AU - Hendrickson, Wayne A.. AU - Rost, Burkhard. PY - 2009/12. Y1 - 2009/12. N2 - The New York Consortium on Membrane Protein Structure (NYCOMPS), a part of the Protein Structure Initiative (PSI) in the USA, has as its mission to establish a high-throughput pipeline for determination of novel integral membrane protein structures. Here we describe our current target selection protocol, which applies structural genomics approaches informed by the collective experience of our team of investigators. We first extract all annotated proteins from our reagent genomes, i.e. the 96 fully sequenced prokaryotic genomes from which we clone DNA. We filter this initial pool of sequences and obtain a list of valid targets. NYCOMPS defines valid targets as those that, among other features, have at ...
TY - CHAP. T1 - The hybrid solution/solid-state NMR method for membrane protein structure determination. AU - Veglia, G.. AU - Traaseth, N. J.. AU - Shi, L.. AU - Verardi, R.. AU - Gopinath, T.. AU - Gustavsson, M.. PY - 2012. Y1 - 2012. N2 - This chapter describes a hybrid nuclear magnetic resonance (NMR) method for the structure determination of membrane proteins. The method consists in combining distance and orientational restraints derived from both solution and solid-state NMR techniques into a hybrid energy function that is minimized using simulated annealing calculations. Using this approach, we are able to determine the structural ensemble, topological orientation, and depth of insertion of membrane proteins in lipid environments. The feasibility of this method is demonstrated for three different single-pass membrane proteins ranging from 3 to 30. kDa in molecular weight. Finally, this chapter provides an overview of the most recent NMR pulse sequences with enhanced sensitivity and ...
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Membrane proteins are proteins that interact with, or are part of, biological membranes. They include integral membrane proteins that are permanently anchored or part of the membrane and peripheral membrane proteins that are only temporarily attached to the lipid bilayer or to other integral proteins.[1][2] The integral membrane proteins are classified as transmembrane proteins that span across the membrane and integral monotopic proteins that are attached to only one side of the membrane. Membrane proteins are a common type of proteins along with soluble globular proteins, fibrous proteins, and disordered proteins.[3] They are targets of over 50% of all modern medicinal drugs.[4] It is estimated that 20-30% of all genes in most genomes encode membrane proteins.[5][6]. Compared to other classes of proteins, the determination of membrane protein structures has remained a challenge in large part due to the difficulty in establishing experimental conditions where the correct conformation of the ...
The topology of the integral membrane protein MalF, which is required for maltose transport in Escherichia coli, has been analyzed using fusions of alkaline phosphatase (EC 3.1.3.1). The properties of such fusion strains support a MalF structure previously proposed on theoretical grounds. Several transmembrane segments within MalF can act as signal sequences in exporting alkaline phosphatase. Other transmembrane sequences, in conjunction with cytoplasmic domains, can stably anchor alkaline phosphatase in the cytoplasm. Our results suggest that features of the amino acid sequence (possibly the positively charged amino acids) of the cytoplasmic domains of membrane proteins are important in anchoring these domains in the cytoplasm. These studies in conjunction with our earlier results show that alkaline phosphatase fusions to membrane proteins can be an important aid in analyzing membrane topology and its determinants.. ...
The overexpression and purification of membrane proteins is a bottleneck in biotechnology and structural biology. E. coli remains the host of choice for membrane protein production. To date, most of the efforts have focused on genetically tuning of expression systems and shaping membrane composition to improve membrane protein production remained largely unexplored. In E. coli C41(DE3) strain, we deleted two transporters involved in fatty acid metabolism (OmpF and AcrB), which are also recalcitrant contaminants crystallizing even at low concentration. Engineered expression hosts presented an enhanced fitness and improved folding of target membrane proteins, which correlated with an altered membrane fluidity. We demonstrated the scope of this approach by overproducing several membrane proteins (4 different ABC transporters, YidC and SecYEG). In summary, E. coli membrane engineering unprecedentedly increases the quality and yield of membrane protein preparations. This strategy opens a new field for
Reliable prediction of structures could have a major impact on our understanding of membrane protein function. This is underscored by the fact that less than 1% of the structures in the Protein Data Bank are of integral membrane proteins despite these comprising over 20% of all genes in mammalian genomes. Membrane proteins are physiologically crucial given their function as a vital communication interface between the intracellular and extracellular environments, and between the cytosol and diverse membrane-bound organelles. Hence, many membrane proteins are pharmacologically important and are potential drug targets. While efforts in structural genomics have led to the elucidation of structures of numerous soluble proteins, determining the structure of membrane proteins remains challenging due to difficulties involved in their expression, purification and crystallization. Thus, any approach that provides insights into structures of membrane proteins will be very useful in explaining their ...
α-helical membrane proteins constitute 20-30% of all proteins in a cell and are involved in many essential cellular functions. The structure is only known for a few hundred of them, which makes structural models important. The most common structural model of a membrane protein is the topology which is a two-dimensional representation of the structure.. This thesis is focused on three different aspects of membrane protein structure: improving structural predictions of membrane proteins, improving the level of detail of structural models and the concept of dual topology.. It is possible to improve topology models of membrane proteins by including experimental information in computer predictions. This was first performed in Escherichia coli and, by using homology, it was possible to extend the results to 225 prokaryotic organisms. The improved models covered ~80% of the membrane proteins in E. coli and ~30% of other prokaryotic organisms.. However, the traditional topology concept is sometimes too ...
From the moment of cotranslational insertion into the lipid bilayer of the endoplasmic reticulum (ER), newly synthesized integral membrane proteins are subject to a complex series of sorting, trafficking, quality control, and quality maintenance systems. Many of these processes are intimately controlled by ubiquitination, a posttranslational modification that directs trafficking decisions related to both the biosynthetic delivery of proteins to the plasma membrane (PM) via the secretory pathway and the removal of proteins from the PM via the endocytic pathway. Ubiquitin modification of integral membrane proteins (or cargoes) generally acts as a sorting signal, which is recognized, captured, and delivered to a specific cellular destination via specialized trafficking events. By affecting the quality, quantity, and localization of integral membrane proteins in the cell, defects in these processes contribute to human diseases, including cystic fibrosis, circulatory diseases, and various ...
Our understanding of the events and cellular components required for the intracellular trafficking, targeting, and degradation of complex multispanning membrane proteins is in its infancy. The study of the life cycle of polytopic membrane proteins has become increasingly important, since improper intracellular trafficking has been implicated in a number of genetic diseases, such as cystic fibrosis, in which the misfolded cystic fibrosis conductance transmembrane regulator (CFTR) chloride channel is retained in the endoplasmic reticulum (ER) or certain forms of hypercholesterolemia in which the mutant low-density lipoprotein receptor is either ER retained or not internalized from the cell surface (1, 24, 52).. This study focuses on the intracellular trafficking of Ste6p, thea-factor mating pheromone transporter in Saccharomyces cerevisiae. Studies on yeast membrane proteins provide excellent model systems for studying general aspects of the trafficking and degradation of distinct classes of ...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Proteins of the p24 family form a rather unique family of abundant, small (20-24 kDa) type I trans-membrane proteins in the early biosynthetic pathway. They can be sub-divided by sequence homology into 4 sub-families (p23 or delta, p24 or beta, p25 or alpha, and p26 or gamma) (Dominguez et al., 1998; Emery et al., 1999). Mammalian cells contain at least one member of each p23, p24 and p25 subfamily, and three members of the p26 sub-family (Emery et al., 1999). All seem to cycle in the early secretory pathway (Blum et al., 1999; Fullekrug et al., 1999; Rojo et al., 2000), and to localize primarily to the cis-Golgi network (CGN) or the cis side of the Golgi complex (Emery et al., 2000; Fullekrug et al., 1999; Rojo et al., 1997; Stamnes et al., 1995), except p25 (GP25L) which is also abundant in the endoplasmic reticulum (ER) (Dominguez et al., 1998; Wada et al., 1991). They share a predicted exoplasmic coiled-coil domain and a small (12-18 amino acids) cytoplasmically oriented C terminus that ...
Creative Biostructure, featured as a leader in the structural biology field, now provides a comprehensive list of custom membrane protein services from gene to structure with an emphasis on protein purification, crystallization, structure determination and analysis.. Although membrane proteins play an important role in all organisms, their purification has historically, and continues to be, a huge challenge for protein scientists. In 2008, 150 unique structures of membrane proteins were available, and by 2019 only 50 human membrane proteins had their structures elucidated. For the important roles they play in cell functions, membrane proteins are now considered to be perfect drug targets. Investigating membrane protein structure and function can provide valuable information for drug characterization and optimization, however, such proteins are inherently difficult to purify and characterize. Even when expressed at high levels, the purification can still be challenging.. Owing to years of devoted ...
My research is on membrane protein structure, dynamics, and function with a focus on membrane proteins involved in bacterial pathogenesis. I teach CHEM4411 and CHEM4421, the Biological Chemistry Laboratory courses at UVa. With my colleagues, Carol Price and Cameron Mura, I have developed a year long inquiry- and research-based biochemistry laboratory. We have created BioLEd to share and enable faculty to more easily develop their undergraduate biochemistry laboratories and research.. ...
The ERM family members, ezrin, radixin, and moesin, localizing just beneath the plasma membranes, are thought to be involved in the actin filament/plasma membrane association. To identify the integral membrane protein directly associated with ERM family members, we performed immunoprecipitation studies using antimoesin mAb and cultured baby hamster kidney (BHK) cells metabolically labeled with [35S]methionine or surface-labeled with biotin. The results indicated that moesin is directly associated with a 140-kD integral membrane protein. Using BHK cells as antigens, we obtained a mAb that recognized the 140-kD membrane protein. We next cloned a cDNA encoding the 140-kD membrane protein and identified it as CD44, a broadly distributed cell surface glycoprotein. Immunoprecipitation with various anti-CD44 mAbs showed that ezrin and radixin, as well as moesin, are associated with CD44, not only in BHK cells, but also in mouse L fibroblasts. Furthermore, immunofluorescence microscopy revealed that in ...
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Creative Biostructure provides custom gene-to-structure services for membrane protein families, unveiling the structures, functions and pharmaceutical properties.
peripheral membrane protein (Science: protein) membrane proteins that are bound to the surface of the membrane and not integrated into the hydrophobic region. Usually soluble and were originally thought to bind to integral proteins by ionic and other weak forces (and could therefore be removed by high ionic strength, for example). However, it is now clear that some peripheral membrane proteins are covalently linked to molecules that are part of the membrane bilayer (see acylated proteins and glypiation) and that there are others that fit the original definition but are perhps more appropriately considered proteins of the cytoskeleton (e.g. Band 4.1 and spectrin) or extracellular matrix (e.g. Fibronectin). ...
The module will cover the structure and function of biological membranes. There will be a general introduction to membrane structure and a discussion of the biosynthesis of membrane proteins. The insertion of membrane proteins into bio-membranes is introduced by matching physic-chemical properties and investigated for spontaneous membrane protein insertion. Protein complexes involved in membrane protein insertion and in transport across the membrane will be introduced. The electron transport chain and its relation to energy transduction will be covered together with an introduction to Mitchells chemi-osmotic hypothesis. The structure and function of specific membrane proteins involved in electron transport, proton translocation and phosphorylation in mitochondria and photosynthesis will be described and discussed in terms of our present understanding of how oxidation reactions or light energy are coupled to the synthesis of ATP. The role of multi-domain cell surface proteins in cell recognition ...
Protein that is physically associated with a membrane, via interactions with lipid headgroups at the membrane surface or with another membrane protein. Peripheral membrane proteins are typically bound to the membrane surface, but may dip slightly into the lipid bilayer. Peripheral membrane protein ...
Despite many high-profile successes, recombinant membrane protein production remains a technical challenge; it is still the case that many fewer membrane protein structures have been published than those of soluble proteins. However, progress is being made because empirical methods have been developed to produce the required quantity and quality of these challenging targets. This review focuses on the microbial expression systems that are a key source of recombinant prokaryotic and eukaryotic membrane proteins for structural studies. We provide an overview of the host strains, tags and promoters that, in our experience, are most likely to yield protein suitable for structural and functional characterization. We also catalogue the detergents used for solubilization and crystallization studies of these proteins. Here, we emphasize a combination of practical methods, not necessarily high-throughput, which can be implemented in any laboratory equipped for recombinant DNA technology and microbial ...
The great majority of helical membrane proteins are inserted co-translationally into the ER membrane through a continuous ribosome-translocon channel. The efficiency of membrane insertion depends on transmembrane (TM) helix amino acid composition, the helix length and the position of the amino acids within the helix. In this work, we conducted a computational analysis of the composition and location of amino acids in transmembrane helices found in membrane proteins of known structure to obtain an extensive set of designed polypeptide segments with naturally occurring amino acid distributions. Then, using an in vitro translation system in the presence of biological membranes, we experimentally validated our predictions by analyzing its membrane integration capacity. Coupled with known strategies to control membrane protein topology, these findings may pave the way to de novo membrane protein design. PubMed: 26987712. Doi: 10.1038/srep23397.. ...
The LPSM works at deciphering the mechanism of membrane-related processes, with a specific emphasis on the molecular mechanism of active transport across biological membranes, as well as the study of protein-protein and protein-lipid interactions and significance. We use a combination of complementary experimental and in silico approaches: biochemistry, spectroscopies, molecular dynamics simulations and structural methods. The laboratory works on flippase-type membrane proteins, on caveolin and on membrane proteins associated with pathologies.
Membrane proteins are of great biomedical importance. They account for ~25% of all genes and are involved in diseases ranging from diabetes to cancer. Membrane proteins play a key role in the biology of infection by pathogens, including both bacteria and viruses. They also play an important role in signalling within and between cells. It is therefore not surprising that membrane proteins are major targets for a wide range of drugs and other therapeutic agents. Recently, the number of known structures of membrane proteins has started to increase. Large scale computer simulations allow researchers to study the movements of these proteins in their native membrane environments. 
A: The fluid mosaic model of membrane structure. The membrane consists of a phospholipid double layer with proteins inserted in it (integral proteins) or bound to the cytoplasmic surface (peripheral proteins). Integral membrane proteins are firmly embedded in the lipid layers. Some of these proteins completely span the bilayer and are called transmembrane proteins, whereas others are embedded in either the outer or inner leaflet of the lipid bilayer. The dotted line in the integral membrane protein is the region where hydrophobic amino acids interact with the hydrophobic portions of the membrane. Many of the proteins and lipids have externally exposed oligosaccharide chains. B: Membrane cleavage occurs when a cell is frozen and fractured (cryofracture). Most of the membrane particles (1) are proteins or aggregates of proteins that remain attached to the half of the membrane adjacent to the cytoplasm (P, or protoplasmic, face of the membrane). Fewer particles are found attached to the outer half ...
Recent increases in the number of deposited membrane protein crystal structures necessitate the use of automated computational tools to position them within the lipid bilayer. Identifying the correct orientation allows us to study the complex relationship between sequence, structure and the lipid environment, which is otherwise challenging to investigate using experimental techniques due to the difficulty in crystallising membrane proteins embedded within intact membranes. We have developed a knowledge-based membrane potential, calculated by the statistical analysis of transmembrane protein structures, coupled with a combination of genetic and direct search algorithms, and demonstrate its use in positioning proteins in membranes, refinement of membrane protein models and in decoy discrimination. Our method is able to quickly and accurately orientate both alpha-helical and beta-barrel membrane proteins within the lipid bilayer, showing closer agreement with experimentally determined values than existing
This project seeks to determine the mechanisms, structures, and structure change of integral transmembrane proteins that govern critical transmembrane processes, at the level that can lead to improved therapeutics for human disease. The premise is that alterations in molecular structures are necessary for the function of transmembrane transporters and gated channels, and are coordinated by regulatory functions. The hypothesis is that understanding the linkage between structure change and function provides a roadmap for therapeutic intervention by organic compounds or Fab fragments generated to stabilize conformational states. A major innovation is the technology and ability to determine atomic structures of membrane proteins and eukaryotic, or human membrane proteins at a resolution sufficient to instruct in the development of therapeutic development of compounds. Principal technologies include X-ray diffraction, electron cryomicroscopy, transport assays, electrophysiology. Three aims focus on ...
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Membrane proteins fulfil a number of tasks in cells, including signalling, cell-cell interaction, and the transportation of molecules. The prominence of these tasks makes membrane proteins an important target for clinical drugs. Because of the decreasing price of sequencing, the number of sequences known is increasing at such a rate that manual annotations cannot compete. Here, topology prediction is a way to provide additional information. It predicts the location and number of transmembrane helices in the protein and the orientation inside the membrane. An important factor to detect transmembrane helices is their hydrophobicity, which can be calculated using dedicated scales. In the first paper, we studied the difference between several hydrophobicity scales and evaluated their performance. We showed that while they appear to be similar, their performance for topology prediction differs significantly. The better performing scales appear to measure the probability of amino acids to be within a ...
Integral membrane proteins (SCAMPs), tetraspan vesicle membrane proteins) that act as carriers, recycling proteins to the cell surface. At least three members of the family have been identified in humans: SCAMP1 (338 aa), SCAMP2 (329 aa), and SCAMP3 (347 aa). ...
TY - JOUR. T1 - Mimicking multipass transmembrane proteins. T2 - Synthesis, assembly and folding of alternating amphiphilic multiblock molecules in liposomal membranes. AU - Muraoka, Takahiro. AU - Shima, Tatsuya. AU - Hamada, Tsutomu. AU - Morita, Masamune. AU - Takagi, Masahiro. AU - Kinbara, Kazushi. PY - 2011/12/6. Y1 - 2011/12/6. N2 - Alternating amphiphilic multiblock molecules 1-4, involving fluorescent hydrophobic units, were designed as mimics for multipass transmembrane proteins. Fluorescence spectroscopy of 1-4 in liposomal membranes suggested the face-to-face stacking of the hydrophobic units to give folded structures as well as intermolecular assemblies.. AB - Alternating amphiphilic multiblock molecules 1-4, involving fluorescent hydrophobic units, were designed as mimics for multipass transmembrane proteins. Fluorescence spectroscopy of 1-4 in liposomal membranes suggested the face-to-face stacking of the hydrophobic units to give folded structures as well as intermolecular ...
To understand the partnership between conformational maturation and quality controlCmediated proteolysis in the secretory pathway, we engineered the well-characterized degron from your -subunit from the T-cell antigen receptor (TCR) in to the -helical transmembrane domain name of homotrimeric type I integral membrane proteins, influenza hemagglutinin (HA). antibodies show that membrane-integrated HA++ substances have the ability to mature towards the plasma membrane having a conformation indistinguishable from that of HAwt. These evidently indigenous HA++ substances are, nevertheless, quickly degraded by an activity thats insensitive to proteasome inhibitors but clogged by lysosomotropic amines. These data recommend the presence in the secretory pathway of at least two sequential quality control checkpoints that identify the same transmembrane degron, therefore making sure the fidelity of proteins deployment towards the plasma membrane. Intro Biogenesis of essential membrane proteins in ...
Proteins and channels , Hydrophobicity , Self-assembly ,,. Hydrophobicity literally means fear of water. The opposite of this is hydrophilicity which means love of water. These two terms denote the properties of molecules or parts of molecules to bond with water (hydrophilicity) or reject water (hydrophobicity). This effect is seen when one puts a drop of oil on water. The oil (hydrophobic) remains on the surface and sticks together in stead of mixing with the water (hydrophilic). In cells these properties are essential. Most of the cell is hydrophilic but there are hydrophobic borders (membranes) which compartmentalize the cell into different spaces and hereby separate reactions. Of course there must be some sort of interaction between compartments and this is facilitated by membrane proteins (look here to read up on membrane proteins).. These membranes are formed with molecules with hydrophobic properties, such as phospholipids, cholesterol and membrane proteins. The phospholipids and ...
Junctional complexes between the plasma membrane (PM) and endoplasmic/sarcoplasmic reticulum (ER/SR) are a common feature of all excitable cell types and mediate cross talk between cell surface and intracellular ion channels. Junctophilins (JPs) are important components of the junctional complexes. JPs are composed of a carboxy-terminal hydrophobic segment spanning the ER/SR membrane and a remaining cytoplasmic domain that shows specific affinity for the PM. Four JPs have been identified as tissue-specific subtypes derived from different genes: JPH1 is expressed in skeletal muscle, JPH2 is detected throughout all muscle cell types, and JPH3 and JPH4 are predominantly expressed in the brain. In the CNS, both JPH3 and JPH4 are expressed throughout neural sites and contribute to the subsurface cistern formation in neurons. Mice lacking both JPH3 and JPH4 subtypes exhibit serious symptoms such as impaired learning and memory and are accompanied by abnormal nervous functions. A repeat expansion in ...
Voltage gated potassium channels are transmembrane protein complexes that form a pore specifically allowing the passage of potassium ions. One method to determine the structure of these and other membrane proteins is electron crystallography. For this, purified membrane proteins are mixed with lipids and induced to form two-dimensional crystals. These flat crystal sheets are then imaged by cryo-EM and analysed. There is no potential gradient across them as the protein is surrounded by the same buffer. The gradient required for voltage gated channel proteins to function can be created if they are embedded in a spherical lipid bilayer that encloses liquid, i.e., if they are embedded in the membrane of a liposome. The buffer conditions inside and outside the liposomes dictate whether they are in an open or a closed conformation ...
Membrane proteins are critical components of all cells, controlling, e.g., signaling, nutrient exchange, and energy production, and are the target of over half of all drugs currently in production. At an early stage of their synthesis, nearly all membrane proteins are directed to a protein-conducting channel, the SecY/Sec61 complex, which permits access to the membrane via its lateral gate.
Within this framework, we focus on several membrane proteins whose function is to transport copper ions for one, chloride ions for another, and whose dysfunctionings are responsible for serious diseases in humans, such as Wilsons disease and cystic fibrosis. Our work focuses also on other membrane proteins responsible for transporting metals (TRP channels as TPRC6 and TRPM7 and P-type ATPases). Another concern of ours is the regulation of metal homeostasis by bacterial transcriptional regulators and eukaryotic translational regulators involved in the homeostatic control of iron and nickel. Studies of these regulatory systems, especially in stress conditions (metallic, oxidative or, for example associated with exposure to nanoparticles or other chemical molecules) is of particular interest to understand the metabolic disturbances caused ...
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Integral membrane proteins are found within the plasma membrane and span the whole length across. The inside of the membrane is very hydrophobic due to the long carbon chains. Extensive hydrophobic interactions between the protein side chain and the lipid tails will help anchor the protein in the membrane.. ...
Presented in this section is an adherent culture of Swiss mouse embryo fibroblasts that was immunofluorescently labeled with Rhodamine Red conjugated to antibodies directed against peroxisomal membrane protein 70 (PMP 70), an abundant and integral membrane component of peroxisomes.
Presented in the digital image in this section is a culture of Swiss mouse embryo fibroblasts that was immunofluorescently labeled with Rhodamine Red conjugated to antibodies directed against peroxisomal membrane protein 70 (PMP 70), an abundant and integral membrane component of peroxisomes.
Membrane Protein Structure and Dynamics - This Methods in Molecular Biology TM book details approaches to the structure dynamics and interactions of membrane (EAN:9781627030229)
JC just returned from two back-to-back meetings in Snowmass, CO. He presented work on small-helix partitioning in membranes at the first meeting on Free Energy Methods and structures of BamA and a new complex between SecY and a nascent chain at the second meeting on Membrane Proteins. Not all the time was spent in front of a screen though, as the picture to the right clearly shows!. ...
The Valiyaveetil lab studies potassium channels, which are integral membrane proteins that catalyze the selective conduction of K+ ions across biological membranes. While a great deal of research has been focused on these channels, fundamental questions regarding the mechanism of ionic selectivity and gating remain. Valiyaveetils team has developed a unique combination of methods to address these questions. Their methods include the use of chemical synthesis to introduce precise chemical changes in the channels, x-ray crystallography to determine the structural effects and electrophysiology to determine the functional effects of these changes. Using this multidisciplinary approach they hope to explain the mechanism of ion selectivity and channel gating.. ...
Membrane proteins play an essential role in controlling the movement of material and information in and out of the cell, in determining the flow and use of energy, as well as in triggering the initiation of numerous signaling pathways. To fulfill these roles, conformational and interaction dynamics exert a dominant influence on their functional behavior, for it is the interplay between structure and dynamics what ultimately defines their function.. The Membrane Protein Structural Dynamics Consortium (MPSDC) has been designed as a highly interactive, tightly integrated and multidisciplinary effort focused on elucidating the relationship between structure, dynamics and function in a variety of membrane proteins. This website serves as a gateway both to the Consortiums activities and resources, and to the scientific field at large. Read the directors statement ». ...
Separation of integral membrane proteins by 2-DE. The integral proteins were separated using 18-cm IPG strips covering pH ranges 3-10 (nonlinear), and 4-7 f
Coll, J M.; Luborsky, S W.; and Mora, P T., Metabolically labeled cell membrane proteins in spontaneously and in sv40 virus transformed mouse fibroblasts. (1977). Subject Strain Bibliography 1977. 1406 ...
Integrins are heterodimers formed by the noncovalent bonding of two transmembrane glycoproteins,ref,You TJ, Maxwell DS, Kogan TP, et al. A 3D structure model of integrin alpha 4 beta 1 complex: I. Construction of a homology model of beta 1 and ligand binding analysis. Biophysical Journal. 2002;82(1 Pt 1):447-457.,/ref,; an alpha and beta subunit. As they are transmembrane proteins, they consist of both a relatively large extracellular component and a short cytoplasmic component. The extracellular component consists of approximately 1000 amino acids for the α (alpha) subunit and 700 amino acids for the β (beta) subunit. About half of the α subunits possess an I-domain region at the β-propeller which is an important binding site for ligands. Ligand protein binding is essential because it is the way integrins interact with actin cytoskeleton organization and initiate the transduction of intracelluar signals. Like the α subunit, the β also possesses an I-domain which functions essentially the ...
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