Results 221 to 230 of about 259,716 (267)
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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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On the Complexity of Protein Folding
Journal of Computational Biology, 1998We show that the protein folding problem in the two-dimensional H-P model is NP-complete.
CRESCENZI, PIERLUIGI +4 more
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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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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
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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
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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
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2010
The existing experimental data on protein folding is briefly reviewed. It is argued that the optimal fit is within a multi-funnel shaped free energy landscape and a kinetic mechanism for folding. The possibility that the transient forces responsible for such a kinetic mechanism come from vibrational excited states (the VES hypothesis) is introduced ...
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The existing experimental data on protein folding is briefly reviewed. It is argued that the optimal fit is within a multi-funnel shaped free energy landscape and a kinetic mechanism for folding. The possibility that the transient forces responsible for such a kinetic mechanism come from vibrational excited states (the VES hypothesis) is introduced ...
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Classification of Protein Folds
Molecular Biotechnology, 2002The diversity and complexity of bioinformatics tools currently available for protein sequence analysis can make it difficult to know where to begin when presented with a new sequence. In this article, we present a protocol outlining one approach to sequence analysis that should give as comprehensive a picture as possible as to the likely structure and ...
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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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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
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