Results 301 to 310 of about 6,771,465 (361)
Some of the next articles are maybe not open access.
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
Amyloid Polymorphism in the Protein Folding and Aggregation Energy Landscape.
Angewandte Chemie, 2018Protein folding involves a large number of steps and conformations in which the folding protein samples different thermodynamic states characterized by local minima.
J. Adamcik, R. Mezzenga
semanticscholar +1 more source
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
openaire +2 more sources
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
openaire +2 more sources
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.
openaire +2 more sources
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.
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
Cotranslational Protein Folding
Molecular Biology, 2001The review analyzes the research concerning the folding of proteins in the course of their synthesis on ribosomes. The experimental data obtained for various proteins using various methods give grounds for concluding that a nascent protein largely acquires its spatial structure while still attached to the ribosome, and final folding into the ...
openaire +2 more sources