Results 221 to 230 of about 3,672,982 (262)
Some of the next articles are maybe not open access.
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
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 ...
David T. Jones, Janet M. Thornton
openaire +3 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 ...
David T. Jones, Janet M. Thornton
openaire +3 more sources
Annual Review of Biochemistry, 1993
Advances in spectroscopy, protein engineering, and peptide synthesis have had a dramatic impact on the understanding of the structures and stabilities of transient folding intermediates. The data available from a variety of proteins point to the existence of three common stages of folding. 1.
openaire +2 more sources
Advances in spectroscopy, protein engineering, and peptide synthesis have had a dramatic impact on the understanding of the structures and stabilities of transient folding intermediates. The data available from a variety of proteins point to the existence of three common stages of folding. 1.
openaire +2 more sources
Chaperones and protein folding
Current Opinion in Cell Biology, 1992Chaperones are centrally involved in the control of protein structure, function, localization and transport. A flurry of scientific activity continues to examine the molecular nature of chaperone-substrate recognition and the role of auxiliary chaperones (cohort proteins) and small molecules that expedite these processes.
Kelley, William, Georgopoulos, C.
openaire +4 more sources
Accounts of Chemical Research, 2000
The oxidative folding of proteins is reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A). The mutual effects of conformational folding and disulfide bond regeneration are emphasized, particularly the "locking in" of native disulfide bonds by stable tertiary structure in disulfide intermediates.
M, Narayan +3 more
openaire +2 more sources
The oxidative folding of proteins is reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A). The mutual effects of conformational folding and disulfide bond regeneration are emphasized, particularly the "locking in" of native disulfide bonds by stable tertiary structure in disulfide intermediates.
M, Narayan +3 more
openaire +2 more sources
Biochemistry (Moscow), 2010
Statistical analysis of protein folding rates has been done for 84 proteins with available experimental data. A surprising result is that the proteins with multi-state kinetics from the size range of 50-100 amino acid residues (a.a.) fold as fast as proteins with two-state kinetics from the same size range. At the same time, the proteins with two-state
openaire +2 more sources
Statistical analysis of protein folding rates has been done for 84 proteins with available experimental data. A surprising result is that the proteins with multi-state kinetics from the size range of 50-100 amino acid residues (a.a.) fold as fast as proteins with two-state kinetics from the same size range. At the same time, the proteins with two-state
openaire +2 more sources
On the Universe of Protein Folds
Annual Review of Biophysics, 2013In the fifty years since the first atomic structure of a protein was revealed, tens of thousands of additional structures have been solved. Like all objects in biology, proteins structures show common patterns that seem to define family relationships. Classification of proteins structures, which started in the 1970s with about a dozen structures, has ...
Rachel, Kolodny +3 more
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
The barriers in protein folding
Nature Structural Biology, 1994Elimination of an interaction which forms in denatured cytochrome c enables the majority of the molecules to fold to the native state on a 15 ms time scale, without populating observable intermediates. These results are contrary to the current view that particular steps in protein folding, including the supposedly rate-limiting molten globule to native
T R, Sosnick +3 more
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