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Journal articles on the topic 'Membrane proteins; Biophysics'

Author: Grafiati
Published: 4 June 2021
Last updated: 8 February 2022

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1

Chin, G. J. "BIOPHYSICS: Deconstructing Membrane Proteins." Science 307, no. 5713 (February 25, 2005): 1173a. http://dx.doi.org/10.1126/science.307.5713.1173a.

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2

Thompson, Lynmarie K., and Merritt Maduke. "Special Issue: Molecular Biophysics of Membranes and Membrane Proteins." Biochimica et Biophysica Acta (BBA) - Biomembranes 1862, no. 1 (January 2020): 183116. http://dx.doi.org/10.1016/j.bbamem.2019.183116.

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3

Sawada, Ryusuke, Runcong Ke, Toshiyuki Tsuji, Masashi Sonoyama, and Shigeki Mitaku. "Ratio of membrane proteins in total proteomes of prokaryota." BIOPHYSICS 3 (2007): 37–45. http://dx.doi.org/10.2142/biophysics.3.37.

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4

Thoma, Johannes, and Björn M. Burmann. "Fake It ‘Till You Make It—The Pursuit of Suitable Membrane Mimetics for Membrane Protein Biophysics." International Journal of Molecular Sciences 22, no. 1 (December 23, 2020): 50. http://dx.doi.org/10.3390/ijms22010050.

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Membrane proteins evolved to reside in the hydrophobic lipid bilayers of cellular membranes. Therefore, membrane proteins bridge the different aqueous compartments separated by the membrane, and furthermore, dynamically interact with their surrounding lipid environment. The latter not only stabilizes membrane proteins, but directly impacts their folding, structure and function. In order to be characterized with biophysical and structural biological methods, membrane proteins are typically extracted and subsequently purified from their native lipid environment. This approach requires that lipid membranes are replaced by suitable surrogates, which ideally closely mimic the native bilayer, in order to maintain the membrane proteins structural and functional integrity. In this review, we survey the currently available membrane mimetic environments ranging from detergent micelles to bicelles, nanodiscs, lipidic-cubic phase (LCP), liposomes, and polymersomes. We discuss their respective advantages and disadvantages as well as their suitability for downstream biophysical and structural characterization. Finally, we take a look at ongoing methodological developments, which aim for direct in-situ characterization of membrane proteins within native membranes instead of relying on membrane mimetics.
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5

Separovic, Frances, J. Antoinette Killian, Myriam Cotten, David D. Busath, and Timothy A. Cross. "Modeling the Membrane Environment for Membrane Proteins." Biophysical Journal 100, no. 8 (April 2011): 2073–74. http://dx.doi.org/10.1016/j.bpj.2011.02.058.

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6

Fischer, Wolfgang B., Gerhard Thiel, and Rainer H. A. Fink. "Viral membrane proteins." European Biophysics Journal 39, no. 7 (August 12, 2009): 1041–42. http://dx.doi.org/10.1007/s00249-009-0525-y.

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7

Garni, Martina, Sagana Thamboo, Cora-Ann Schoenenberger, and Cornelia G. Palivan. "Biopores/membrane proteins in synthetic polymer membranes." Biochimica et Biophysica Acta (BBA) - Biomembranes 1859, no. 4 (April 2017): 619–38. http://dx.doi.org/10.1016/j.bbamem.2016.10.015.

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8

Smith, Steven O., Kathryn Aschheim, and Michel Groesbeek. "Magic angle spinning NMR spectroscopy of membrane proteins." Quarterly Reviews of Biophysics 29, no. 4 (December 1996): 395–449. http://dx.doi.org/10.1017/s0033583500005898.

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The passage of molecules and information across cell membranes is mediated largely by membrane-spanning proteins acting as channels, pumps, receptors and enzymes. These proteins perform many tasks: they control electrochemical gradients across the membrane, receive signals from the environment or from other cells, convert light energy into chemical signals, transport small molecules into and out of cells, and harness proton gradients to generate the energy consumed in metabolism. Indeed, of the estimated 50000–100000 genes in the human genome, fully 20–40 % are thought to encode integral membrane proteins. If one also includes membrane-associated proteins, which are attached to the membrane surface through fatty acyl chains or electrostatic interactions, this percentage is likely to be much higher.
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9

Fischer, Wolfgang B. "Assembling Within The Lipid Membrane: Viral Membrane Proteins." Biophysical Journal 96, no. 3 (February 2009): 338a—339a. http://dx.doi.org/10.1016/j.bpj.2008.12.3823.

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10

Lavi, Yael, Michael A. Edidin, and Levi A. Gheber. "Dynamic Patches of Membrane Proteins." Biophysical Journal 93, no. 6 (September 2007): L35—L37. http://dx.doi.org/10.1529/biophysj.107.111567.

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11

Joh, Nathan H., Duan Yang, Andrew Min, and James Bowie. "Forces that stabilize membrane proteins." Biophysical Journal 96, no. 3 (February 2009): 334a. http://dx.doi.org/10.1016/j.bpj.2008.12.1681.

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12

Schlebach, Jonathan P., and Charles R. Sanders. "The safety dance: biophysics of membrane protein folding and misfolding in a cellular context." Quarterly Reviews of Biophysics 48, no. 1 (November 25, 2014): 1–34. http://dx.doi.org/10.1017/s0033583514000110.

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AbstractMost biological processes require the production and degradation of proteins, a task that weighs heavily on the cell. Mutations that compromise the conformational stability of proteins place both specific and general burdens on cellular protein homeostasis (proteostasis) in ways that contribute to numerous diseases. Efforts to elucidate the chain of molecular events responsible for diseases of protein folding address one of the foremost challenges in biomedical science. However, relatively little is known about the processes by which mutations prompt the misfolding of α-helical membrane proteins, which rely on an intricate network of cellular machinery to acquire and maintain their functional structures within cellular membranes. In this review, we summarize the current understanding of the physical principles that guide membrane protein biogenesis and folding in the context of mammalian cells. Additionally, we explore how pathogenic mutations that influence biogenesis may differ from those that disrupt folding and assembly, as well as how this may relate to disease mechanisms and therapeutic intervention. These perspectives indicate an imperative for the use of information from structural, cellular, and biochemical studies of membrane proteins in the design of novel therapeutics and in personalized medicine.
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13

Wang, Sheng, Zongan Wang, John Jumper, Karl F. Freed, Tobin R. Sosnick, and Jinbo Xu. "Folding Membrane Proteins by Contacts Inferred from Non-Membrane Proteins and Near-Atomic Level Refinement." Biophysical Journal 112, no. 3 (February 2017): 204a—205a. http://dx.doi.org/10.1016/j.bpj.2016.11.1130.

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14

Vogel, Horst. "Structure and dynamics of polypeptides and proteins in lipid membranes." Quarterly Reviews of Biophysics 25, no. 4 (November 1992): 433–57. http://dx.doi.org/10.1017/s0033583500004364.

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The elucidation of the molecular mechanisms whereby ions and polar molecules are translocated across the hydrophobic barrier of a lipid bilayer in biological membranes is one of the most challenging problems in biological research. Specific membrane proteins, such as pumps, carriers and channels, play the central role in the various translocation pathways. Recent progress in expression cloning has provided the sequence of a number of biologically important membrane proteins and in principle the door is open to investigate every protein which might be of importance in the central signal transduction and transport processes. Unfortunately, to date there are only a few examples where the three-dimensional structure of membrane proteins are known at atomic resolution. The photosynthetic reaction centres from purple bacteria (Deisenhoferet al.1985), bacteriorhodopsin (Hendersonet al.1990) and the large porin channel ofRhodobacter capsulata(Weisset al.1991). According to these structural data membrane proteins seem to fold in general in membrane-spanning α-helices and β-strands in order to saturate hydrogen bonds. Only these two motifs seem to form stable structures which can be in contact with the hydrophobic lipid interior of a membrane.
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15

Matkó, Janos, Janos Szöllösi, Lajos Trón, and Sandor Damjanovich. "Luminescence spectroscopic approaches in studying cell surface dynamics." Quarterly Reviews of Biophysics 21, no. 4 (November 1988): 479–544. http://dx.doi.org/10.1017/s0033583500004637.

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The major elements of membranes, such as proteins, lipids and polysaccharides, are in dynamic interaction with each other (Albertset al.1983). Protein diffusion in the lipid matrix of the membrane, the lipid diffusion and dynamic domain formation below and above their transition temperature from gel to fluid state, have many functional implications. This type of behaviour of membranes is often summarized in one frequently used word membrane fluidity (coined by Shinitzky & Henkart, 1979). The dynamic behaviour of the cell membrane includes rotational, translational and segmental movements of membrane elements (or their domain-like associations) in the plane of, and perpendicular to the membrane. The ever changing proximity relationships form a dynamic pattern of lipids, proteins and saccharide moieties and are usually described as ‘cell-surface dynamics’ (Damjanovichet al.1981). The knowledge about the above defined behaviour originates from experiments performed mostly on cytoplasmic membranes of eukaryotic cells. Nevertheless numerous data are available also on the mitochondrial and nuclear membranes, as well as endo (sarco-)plasmic reticulum (Martonosi, 1982; Slater, 1981; Siekevitz, 1981).
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16

Marsh, Derek. "Interactions at the Membrane Surface Studied by Spin Label ESR Spectroscopy." Bioscience Reports 19, no. 4 (August 1, 1999): 253–59. http://dx.doi.org/10.1023/a:1020590122846.

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A range of different types of interactions at biological membrane surfaces have been studied using various different spin label electron spin resonance (ESR) techniques. These include: (1) the interfacial ionization of local anaesthetics, (2) the binding of peripheral membrane proteins, (3) the membrane insertion of translocation-competent precursor proteins and other components of the protein translocation machinery, (4) the interactions of ganglioside sphingolipids with membrane proteins, and (5) the specific surface recognition of biotinylated phospholipid headgroups by avidin. A description of these illustrates both the capabilities of this biophysical methodology and the functional/technological implications of these interactions and dynamic/thermodynamic processes for cell membranes and their surfaces.
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17

Jap, Bing K., and Peter J. Walian. "Biophysics of the structure and function of porins." Quarterly Reviews of Biophysics 23, no. 4 (November 1990): 367–403. http://dx.doi.org/10.1017/s003358350000559x.

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Gram-negative bacteria such asEscherichia coli(E. coli) andSalmonella typhimurium(S. typhimurium) have two layers of membranes in the cellular envelope – the cytoplasmic membrane and the outer membrane (Fig. I). Between these membranes is a periplasmic space in which there is a peptidoglycan layer that provides the cells with mechanical rigidity. In this periplasmic space, there are also a variety of hydrolases and binding proteins. The composition of the outer membrane is somewhat unusual. This membrane bilayer is asymmetric, having an inner (periplasmic) leaflet composed of phospholipids and an outer (extracellular) leaflet formed by lipopolysaccharide (LPS). Unlike phospholipids having two acyl chains, LPS has six or seven saturated fatty acid chains (see reviews, Lugtenberg & Van Alphen, 1983; Nikaido & Vaara, 1985; Nakae, 1986). The head groups of LPS have a strong affinity for divalent cations such as Ca2+, and given a sufficient concentration of these ions the outer membrane can form quite a formidable permeability barrier through this head group/salt bridge network (Nikaido & Vaara, 1985). The function of the outer membrane is to serve as a protective envelope against hostile environments such as those in the intestinal tract of animals where harmful and toxic substances - for example, bile salts and various enzymes - are often found. The outer membrane itself would be impermeable to most hydrophilic solutes were it not for the presence of membrane channels. The presence of a large number of pore-forming proteins provides both specific and nonspecific diffusion pathways across the outer membrane for solutes such as nutrients and waste products to diffuse into or out of the cell.
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18

Pringle, Alastair T., and John Bramhall. "Bilayer Penetration by Membrane-Associated Proteins." Biophysical Journal 49, no. 1 (January 1986): 102–6. http://dx.doi.org/10.1016/s0006-3495(86)83610-4.

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19

Abney, J. R., B. A. Scalettar, and J. C. Owicki. "Mutual diffusion of interacting membrane proteins." Biophysical Journal 56, no. 2 (August 1989): 315–26. http://dx.doi.org/10.1016/s0006-3495(89)82678-5.

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20

Abney, J. R., B. A. Scalettar, and J. C. Owicki. "Self diffusion of interacting membrane proteins." Biophysical Journal 55, no. 5 (May 1989): 817–33. http://dx.doi.org/10.1016/s0006-3495(89)82882-6.

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21

Kühlbrandt, W. "Three-dimensional crystallization of membrane proteins." Quarterly Reviews of Biophysics 21, no. 4 (November 1988): 429–77. http://dx.doi.org/10.1017/s0033583500004625.

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As recently as 10 years ago, the prospect of solving the structure of any membrane protein by X-ray crystallography seemed remote. Since then, the threedimensional (3-D) structures of two membrane protein complexes, the bacterial photosynthetic reaction centres of Rhodopseudomonas viridis (Deisenhofer et al. 1984, 1985) and of Rhodobacter sphaeroides (Allen et al. 1986, 1987 a, 6; Chang et al. 1986) have been determined at high resolution. This astonishing progress would not have been possible without the pioneering work of Michel and Garavito who first succeeded in growing 3-D crystals of the membrane proteins bacteriorhodopsin (Michel & Oesterhelt, 1980) and matrix porin (Garavito & Rosenbusch, 1980). X-ray crystallography is still the only routine method for determining the 3-D structures of biological macromolecules at high resolution and well-ordered 3-D crystals of sufficient size are the essential prerequisite.
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22

Kühlbrandt, W. "Two-dimensional crystallization of membrane proteins." Quarterly Reviews of Biophysics 25, no. 1 (February 1992): 1–49. http://dx.doi.org/10.1017/s0033583500004716.

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In spite of several great breakthroughs, the overall rate of progress in determining high-resolution structures of membrane proteins has been slow. This is entirely due to the scarcity of suitable, well-ordered crystals. Most membrane proteins are multimeric complexes with a composite molecular mass in excess of 50000 Da which puts them outside the range of current solution NMR techniques. For the foreseeable future, detailed information about the structure of large membrane proteins will therefore depend on crystallographic methods.
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23

Kress, Holger, Rostislav Boltyanskiy, Alexia A. Belperron, Cecile O. Mejean, Charles W. Wolgemuth, Linda K. Bockenstedt, and Eric R. Dufresne. "Ballistic Motion of Spirochete Membrane Proteins." Biophysical Journal 100, no. 3 (February 2011): 515a. http://dx.doi.org/10.1016/j.bpj.2010.12.3013.

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24

Guigas, Gernot, Diana Morozova, and Matthias Weiss. "Dynamic Structure Formation of Membrane Proteins." Biophysical Journal 100, no. 3 (February 2011): 339a. http://dx.doi.org/10.1016/j.bpj.2010.12.2055.

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25

Zeno, Wade F., Upayan Baul, Wilton T. Snead, Andre C. M. DeGroot, Liping Wang, Eileen M. Lafer, Dave Thirumalai, and Jeanne C. Stachowiak. "Intrinsically Disordered Proteins Sense Membrane Curvature." Biophysical Journal 116, no. 3 (February 2019): 21a. http://dx.doi.org/10.1016/j.bpj.2018.11.153.

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26

Busch, David J., Justin R. Houser, Carl C. Hayden, Michael B. Sherman, Eileen M. Lafer, and Jeanne C. Stachowiak. "Intrinsically Disordered Proteins Drive Membrane Curvature." Biophysical Journal 110, no. 3 (February 2016): 37a—38a. http://dx.doi.org/10.1016/j.bpj.2015.11.270.

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27

Semrau, Stefan, Timon Idema, Cornelis Storm, and Thomas Schmidt. "How Membrane Curvature Can Sort Proteins." Biophysical Journal 96, no. 3 (February 2009): 364a. http://dx.doi.org/10.1016/j.bpj.2008.12.1959.

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28

Lan, Tien-Hung, and Nevin A. Lambert. "Diffusion-Enhanced FRET between Membrane Proteins." Biophysical Journal 104, no. 2 (January 2013): 681a—682a. http://dx.doi.org/10.1016/j.bpj.2012.11.3763.

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29

Bradley, Ryan, Natesan Ramakrishnan, Yuting Zhao, Wei Guo, and Ravi Radhakrishnan. "Membrane Remodeling by Curvature-Inducing Proteins." Biophysical Journal 104, no. 2 (January 2013): 98a. http://dx.doi.org/10.1016/j.bpj.2012.11.581.

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30

Kimble-Hill, Ann, Sumit Garg, Amanda Siegel, Rainer Jordan, and Christoph Naumann. "Raft recruitment of Membrane Proteins by Native Ligands and GPI-Anchored Proteins: A Model Membrane Study." Biophysical Journal 96, no. 3 (February 2009): 549a. http://dx.doi.org/10.1016/j.bpj.2008.12.2974.

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31

Seifert, K., K. Fendler, and E. Bamberg. "Charge transport by ion translocating membrane proteins on solid supported membranes." Biophysical Journal 64, no. 2 (February 1993): 384–91. http://dx.doi.org/10.1016/s0006-3495(93)81379-1.

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32

Askarova, Sholpan, Xiaoguang Yang, and James C. M. Lee. "Impacts of Membrane Biophysics in Alzheimer's Disease: From Amyloid Precursor Protein Processing to AβPeptide-Induced Membrane Changes." International Journal of Alzheimer's Disease 2011 (2011): 1–12. http://dx.doi.org/10.4061/2011/134971.

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An increasing amount of evidence supports the notion that cytotoxic effects of amyloid-βpeptide (Aβ), the main constituent of senile plaques in Alzheimer's disease (AD), are strongly associated with its ability to interact with membranes of neurons and other cerebral cells. Aβis derived from amyloidogenic cleavage of amyloid precursor protein (AβPP) byβ- andγ-secretase. In the nonamyloidogenic pathway, AβPP is cleaved byα-secretases. These two pathways compete with each other, and enhancing the non-amyloidogenic pathway has been suggested as a potential pharmacological approach for the treatment of AD. Since AβPP,α-,β-, andγ-secretases are membrane-associated proteins, AβPP processing and Aβproduction can be affected by the membrane composition and properties. There is evidence that membrane composition and properties, in turn, play a critical role in Aβcytotoxicity associated with its conformational changes and aggregation into oligomers and fibrils. Understanding the mechanisms leading to changes in a membrane's biophysical properties and how they affect AβPP processing and Aβtoxicity should prove to provide new therapeutic strategies for prevention and treatment of AD.
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33

Misawa, Nobuo, Toshihisa Osaki, and Shoji Takeuchi. "Membrane protein-based biosensors." Journal of The Royal Society Interface 15, no. 141 (April 2018): 20170952. http://dx.doi.org/10.1098/rsif.2017.0952.

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This review highlights recent development of biosensors that use the functions of membrane proteins. Membrane proteins are essential components of biological membranes and have a central role in detection of various environmental stimuli such as olfaction and gustation. A number of studies have attempted for development of biosensors using the sensing property of these membrane proteins. Their specificity to target molecules is particularly attractive as it is significantly superior to that of traditional human-made sensors. In this review, we classified the membrane protein-based biosensors into two platforms: the lipid bilayer-based platform and the cell-based platform. On lipid bilayer platforms, the membrane proteins are embedded in a lipid bilayer that bridges between the protein and a sensor device. On cell-based platforms, the membrane proteins are expressed in a cultured cell, which is then integrated in a sensor device. For both platforms we introduce the fundamental information and the recent progress in the development of the biosensors, and remark on the outlook for practical biosensing applications.
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34

Nicholls, Peter. "Membrane proteins: Structure, function, assembly." Cell Biophysics 16, no. 1-2 (January 1990): 99–103. http://dx.doi.org/10.1007/bf02989695.

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35

Mandala, Venkata S., Jonathan K. Williams, and Mei Hong. "Structure and Dynamics of Membrane Proteins from Solid-State NMR." Annual Review of Biophysics 47, no. 1 (May 20, 2018): 201–22. http://dx.doi.org/10.1146/annurev-biophys-070816-033712.

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Solid-state nuclear magnetic resonance (SSNMR) spectroscopy elucidates membrane protein structures and dynamics in atomic detail to yield mechanistic insights. By interrogating membrane proteins in phospholipid bilayers that closely resemble biological membranes, SSNMR spectroscopists have revealed ion conduction mechanisms, substrate transport dynamics, and oligomeric interfaces of seven-transmembrane helix proteins. Research has also identified conformational plasticity underlying virus-cell membrane fusions by complex protein machineries, and β-sheet folding and assembly by amyloidogenic proteins bound to lipid membranes. These studies collectively show that membrane proteins exhibit extensive structural plasticity to carry out their functions. Because of the inherent dependence of NMR frequencies on molecular orientations and the sensitivity of NMR frequencies to dynamical processes on timescales from nanoseconds to seconds, SSNMR spectroscopy is ideally suited to elucidate such structural plasticity, local and global conformational dynamics, protein-lipid and protein-ligand interactions, and protonation states of polar residues. New sensitivity-enhancement techniques, resolution enhancement by ultrahigh magnetic fields, and the advent of 3D and 4D correlation NMR techniques are increasingly aiding these mechanistically important structural studies.
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36

Oppenheimer, Naomi, and Haim Diamant. "Correlated Diffusion of Membrane Proteins and Their Effect on Membrane Viscosity." Biophysical Journal 96, no. 8 (April 2009): 3041–49. http://dx.doi.org/10.1016/j.bpj.2009.01.020.

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37

Brumovska, Veronika, Gergö Fülöp, Gerhard J. Schütz, and Eva Sevcsik. "Probing the Membrane Environment of Plasma Membrane Proteins: A Micropatterning Approach." Biophysical Journal 120, no. 3 (February 2021): 279a—280a. http://dx.doi.org/10.1016/j.bpj.2020.11.1778.

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38

Hsiao, Kai-Hung, and Ling Chao. "Using Magnetic Field to Purify Membrane Proteins in Supported Cell Plasma Membranes." Biophysical Journal 112, no. 3 (February 2017): 153a. http://dx.doi.org/10.1016/j.bpj.2016.11.839.

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39

Hansen, Jesper S., and Claus H. Nielsen. "Giant Protein Vesicles for Studying Membrane Proteins." Biophysical Journal 100, no. 3 (February 2011): 338a. http://dx.doi.org/10.1016/j.bpj.2010.12.2051.

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40

Galietta, Luis J. V. "TMEM16 Proteins: Membrane Channels with Unusual Pores." Biophysical Journal 111, no. 9 (November 2016): 1821–22. http://dx.doi.org/10.1016/j.bpj.2016.09.033.

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41

Leiding, Thom, Sergei Vinogradov, Cecilia Hägerhäll, and Sindra Peterson Årsköld. "Probing membrane proteins: Monitoring proton-translocation quantitatively." Biophysical Journal 96, no. 3 (February 2009): 246a. http://dx.doi.org/10.1016/j.bpj.2008.12.1211.

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42

Aleksandrova, Antoniya A., Edoardo Sarti, Emily L. Yaklich, and Lucy R. Forrest. "Systematic Analysis of Symmetry in Membrane Proteins." Biophysical Journal 120, no. 3 (February 2021): 210a. http://dx.doi.org/10.1016/j.bpj.2020.11.1425.

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43

Simunovic, Mijo, Coline Prévost, Andrew Callan-Jones, and Patricia Bassereau. "Physical basis of some membrane shaping mechanisms." Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 374, no. 2072 (July 28, 2016): 20160034. http://dx.doi.org/10.1098/rsta.2016.0034.

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In vesicular transport pathways, membrane proteins and lipids are internalized, externalized or transported within cells, not by bulk diffusion of single molecules, but embedded in the membrane of small vesicles or thin tubules. The formation of these ‘transport carriers’ follows sequential events: membrane bending, fission from the donor compartment, transport and eventually fusion with the acceptor membrane. A similar sequence is involved during the internalization of drug or gene carriers inside cells. These membrane-shaping events are generally mediated by proteins binding to membranes. The mechanisms behind these biological processes are actively studied both in the context of cell biology and biophysics. Bin/amphiphysin/Rvs (BAR) domain proteins are ideally suited for illustrating how simple soft matter principles can account for membrane deformation by proteins. We review here some experimental methods and corresponding theoretical models to measure how these proteins affect the mechanics and the shape of membranes. In more detail, we show how an experimental method employing optical tweezers to pull a tube from a giant vesicle may give important quantitative insights into the mechanism by which proteins sense and generate membrane curvature and the mechanism of membrane scission. This article is part of the themed issue ‘Soft interfacial materials: from fundamentals to formulation’.
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44

Boonstra, Sander, Jelle S. Blijleven, Wouter H. Roos, Patrick R. Onck, Erik van der Giessen, and Antoine M. van Oijen. "Hemagglutinin-Mediated Membrane Fusion: A Biophysical Perspective." Annual Review of Biophysics 47, no. 1 (May 20, 2018): 153–73. http://dx.doi.org/10.1146/annurev-biophys-070317-033018.

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Influenza hemagglutinin (HA) is a viral membrane protein responsible for the initial steps of the entry of influenza virus into the host cell. It mediates binding of the virus particle to the host-cell membrane and catalyzes fusion of the viral membrane with that of the host. HA is therefore a major target in the development of antiviral strategies. The fusion of two membranes involves high activation barriers and proceeds through several intermediate states. Here, we provide a biophysical description of the membrane fusion process, relating its kinetic and thermodynamic properties to the large conformational changes taking place in HA and placing these in the context of multiple HA proteins working together to mediate fusion. Furthermore, we highlight the role of novel single-particle experiments and computational approaches in understanding the fusion process and their complementarity with other biophysical approaches.
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45

Öjemyr, Linda, Tor Sandén, Jerker Widengren, and Peter Brzezinski. "S13.23 Proton transfer along surfaces of membranes and membrane-proteins." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1777 (July 2008): S94. http://dx.doi.org/10.1016/j.bbabio.2008.05.367.

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46

Riznichenk, Galina, Ilya Kovalenko, Vladimir Fedorov, Sergei Khruschev, and Andrey Rubin. "Photosynthetic Electron Transfer by Dint of Protein Mobile Carriers. Multi-particle Brownian and Molecular Modeling." EPJ Web of Conferences 224 (2019): 03008. http://dx.doi.org/10.1051/epjconf/201922403008.

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The paper presents the review of works on modeling the interaction of photosynthetic proteins using the multiparticle Brownian dynamics method developed at the Department of Biophysics, Biological Faculty, Lomonosov Moscow State University. The method describes the displacement of individual macromolecules – mobile electron carriers, and their electrostatic interactions between each other and with pigment-protein complexes embedded in photosynthetic membrane. Three-dimensional models of the protein molecules were constructed on the basis of the data from the Protein Data Bank. We applied the Brownian methods coupled to molecular dynamic simulations to reveal the role of electrostatic interactions and conformational motions in the transfer of an electron from the cytochrome complex Cyt b6f) membrane we developed the model which combines events of proteins Pc diffusion along the thylakoid membrane, electrostatic interactions of Pc with the membrane charges, formation of Pc super-complexes with multienzyme complexes of Photosystem I and to the molecule of the mobile carrier plastocyanin (Pc) in plants, green algae and cyanic bacteria. Taking into account the interior of photosynthetic membrane we developed the model which combines events of proteins Pc diffusion along the thylakoid membrane, electrostatic interactions of Pc with the membrane charges, formation of Pc super-complexes with multienzyme complexes of Photosystem I and Cyt b6f, embedded in photosynthetic membrane, electron transfer and complex dissociation. Multiparticle Brownian simulation method can be used to consider the processes of protein interactions in subcellular systems in order to clarify the role of individual stages and the biophysical mechanisms of these processes.
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47

Lin Goh, Shih, Qi Wang, and Holger Sondermann. "Membrane Properties Influence the Membrane Deformation Activity Mediated by BAR Domain Proteins." Biophysical Journal 98, no. 3 (January 2010): 500a. http://dx.doi.org/10.1016/j.bpj.2009.12.2723.

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48

Nakao, Hiroyuki, Keisuke Ikeda, Yasushi Ishihama, and Minoru Nakano. "Flip-Flop Promotion by Membrane-Spanning Sequences in the ER Membrane Proteins." Biophysical Journal 110, no. 3 (February 2016): 567a. http://dx.doi.org/10.1016/j.bpj.2015.11.3033.

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49

González Flecha, F. Luis. "Kinetic stability of membrane proteins." Biophysical Reviews 9, no. 5 (September 18, 2017): 563–72. http://dx.doi.org/10.1007/s12551-017-0324-0.

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50

Heijne, G. V. "Membrane Proteins: From Sequence to Structure." Annual Review of Biophysics and Biomolecular Structure 23, no. 1 (June 1994): 167–92. http://dx.doi.org/10.1146/annurev.bb.23.060194.001123.

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