Results 221 to 230 of about 255,418 (267)
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Quarterly Reviews of Biophysics, 1977
This review describes recent advances in studies on the stabilities of the three-dimensional structures of proteins and on the processes leading to the formation of these structures. The term ‘protein folding’ will be used here to denote the process of the conversion of an open polypeptide chain into the unique three-dimensional conformation of the ...
G, Némethy, H A, Scheraga
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This review describes recent advances in studies on the stabilities of the three-dimensional structures of proteins and on the processes leading to the formation of these structures. The term ‘protein folding’ will be used here to denote the process of the conversion of an open polypeptide chain into the unique three-dimensional conformation of the ...
G, Némethy, H A, Scheraga
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Annual Review of Biochemistry, 1981
After some general remarks on protein structure, there follows a discussion on primary, secondary, and tertiary organization. The account of primary structure includes a discussion of the conformation of disulfide bonds. Types of helices, sheets, and turns are described in the section on secondary structure, followed by a discussion of super-secondary ...
M G, Rossmann, P, Argos
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After some general remarks on protein structure, there follows a discussion on primary, secondary, and tertiary organization. The account of primary structure includes a discussion of the conformation of disulfide bonds. Types of helices, sheets, and turns are described in the section on secondary structure, followed by a discussion of super-secondary ...
M G, Rossmann, P, Argos
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How Fast-Folding Proteins Fold
Science, 2011Millisecond-scale molecular dynamics simulations of 12 proteins reveal a set of common principles for protein folding.
Kresten, Lindorff-Larsen +3 more
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Protein structures, folds and fold spaces
Journal of Physics: Condensed Matter, 2009There has been considerable progress towards the goal of understanding the space of possible tertiary structures adopted by proteins. Despite a greatly increased rate of structure determination and a deliberate strategy of sequencing proteins expected to be very different from those already known, it is now rare to see a genuinely new fold, leading to ...
Michael I, Sadowski, William R, Taylor
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Journal of Computer-Aided Molecular Design, 1993
An important, yet seemingly unattainable, goal in structural molecular biology is to be able to predict the native three-dimensional structure of a protein entirely from its amino acid sequence. Prediction methods based on rigorous energy calculations have not yet been successful, and best results have been obtained from homology modelling and ...
D, Jones, J, Thornton
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An important, yet seemingly unattainable, goal in structural molecular biology is to be able to predict the native three-dimensional structure of a protein entirely from its amino acid sequence. Prediction methods based on rigorous energy calculations have not yet been successful, and best results have been obtained from homology modelling and ...
D, Jones, J, Thornton
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Nature, 1976
In a discussion of the dynamics of protein folding two limiting models (random-search nucleation and chain propagation., diffusion–collision) are considered. It is suggested that the latter may have the dominant role in many proteins.
M, Karplus, D L, Weaver
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In a discussion of the dynamics of protein folding two limiting models (random-search nucleation and chain propagation., diffusion–collision) are considered. It is suggested that the latter may have the dominant role in many proteins.
M, Karplus, D L, Weaver
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Journal of Theoretical Biology, 2008
We investigate the average inter-residue folding forces derived from mutational data of the 15 proteins: barstar, barnase, chymotrypsin inhibitor 2 (CI2), Src SH3 domain, spectrin R16 domain, Arc repressor, apo-azurin, cold shock protein B (cspB), C-terminal domain of ribosomal protein L9 (CTL9), FKBP12, alpha-lactalbumin, colicin E7 immunity protein 7
Bengt, Nölting +2 more
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We investigate the average inter-residue folding forces derived from mutational data of the 15 proteins: barstar, barnase, chymotrypsin inhibitor 2 (CI2), Src SH3 domain, spectrin R16 domain, Arc repressor, apo-azurin, cold shock protein B (cspB), C-terminal domain of ribosomal protein L9 (CTL9), FKBP12, alpha-lactalbumin, colicin E7 immunity protein 7
Bengt, Nölting +2 more
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Biochemistry, 1996
Proline isomerization, an intrinsically slow process, kinetically traps intermediates in slow protein folding reactions. Thus, enzymes that catalyze proline isomerization (prolyl isomerases) often catalyze protein folding. We have investigated the folding kinetics of FKBP, a prolyl isomerase.
S, Veeraraghavan +2 more
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Proline isomerization, an intrinsically slow process, kinetically traps intermediates in slow protein folding reactions. Thus, enzymes that catalyze proline isomerization (prolyl isomerases) often catalyze protein folding. We have investigated the folding kinetics of FKBP, a prolyl isomerase.
S, Veeraraghavan +2 more
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ChemInform, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
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AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
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Current Opinion in Structural Biology, 1999
Investigating the in vitro refolding of proteins that naturally reside in biological membranes is a notoriously difficult task. Biophysical studies on model systems are beginning to provide a sound physical basis for membrane protein folding that should help to alleviate this problem. Highlights of these studies include insights into the interaction of
P J, Booth, A R, Curran
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Investigating the in vitro refolding of proteins that naturally reside in biological membranes is a notoriously difficult task. Biophysical studies on model systems are beginning to provide a sound physical basis for membrane protein folding that should help to alleviate this problem. Highlights of these studies include insights into the interaction of
P J, Booth, A R, Curran
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