Results 341 to 350 of about 6,834,568 (390)
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European Biophysics Journal, 2008
Understanding the mechanism by which a polypeptide chain folds into its native structure is a central problem of modern biophysics. The collaborative efforts of experimental and theoretical studies recently raised the tantalizing possibility to define a unifying mechanism for protein folding.
IVARSSON Y +3 more
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Understanding the mechanism by which a polypeptide chain folds into its native structure is a central problem of modern biophysics. The collaborative efforts of experimental and theoretical studies recently raised the tantalizing possibility to define a unifying mechanism for protein folding.
IVARSSON Y +3 more
openaire +6 more sources
Principles that govern the folding of protein chains.
Science, 1973Stanford Moore, William Stein, and Anfinsen were awarded the Nobel Prize in Chemistry in 1972 for "their contribution to the understanding of the connection between chemical structure and catalytic activity of the active center of the ribonuclease ...
C. Anfinsen
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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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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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How Fast-Folding Proteins Fold
Science, 2011Millisecond-scale molecular dynamics simulations of 12 proteins reveal a set of common principles for protein folding.
Ron O. Dror +4 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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Molecular chaperone functions in protein folding and proteostasis.
Annual Review of Biochemistry, 2013The biological functions of proteins are governed by their three-dimensional fold. Protein folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically depend on a complex network of molecular chaperones.
Yujin E. Kim +4 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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Bulletin of Mathematical Biology, 1993
It is believed that the native folded three-dimensional conformation of a protein is its lowest free energy state, or one of its lowest. It is shown here that both a two- and three-dimensional mathematical model describing the folding process as a free energy minimization problem is NP-hard.
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It is believed that the native folded three-dimensional conformation of a protein is its lowest free energy state, or one of its lowest. It is shown here that both a two- and three-dimensional mathematical model describing the folding process as a free energy minimization problem is NP-hard.
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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.
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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 +3 more sources