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Protein-catalysed protein folding
Trends in Biotechnology, 1990A number of proteins, termed chaperonins, have been identified as part of the mechanism of folding other proteins into their biologically active forms. The role of chaperonins appears to be twofold--to prevent illegitimate interactions with other proteins and to facilitate folding, possibly through an energy-dependent, catalytic function.
A L, Horwich, W, Neupert, F U, Hartl
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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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2008
Publisher Summary This chapter reexamines the problem of protein folding in view of the earlier convenient folding models but in a modern format. With powerful computers, folding simulators today need to get away from explaining their work so much in terms of a long standing energy landscape model, which is incomplete. The amino acid sequence somehow
Barry, Robson, Andy, Vaithilingam
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Publisher Summary This chapter reexamines the problem of protein folding in view of the earlier convenient folding models but in a modern format. With powerful computers, folding simulators today need to get away from explaining their work so much in terms of a long standing energy landscape model, which is incomplete. The amino acid sequence somehow
Barry, Robson, Andy, Vaithilingam
openaire +2 more sources
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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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.
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Protein Folding: Folding helpers and unhelpful folders
Current Biology, 1994Recent studies have provided new insights into the mode of action of protein disulphide isomerases in the catalysis of protein folding.
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Proteins: Structure, Function, and Bioinformatics, 1991
A. Nicholls, K. Sharp, B. Honig
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A. Nicholls, K. Sharp, B. Honig
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Molecular chaperones in protein folding and proteostasis
Nature, 2011F. Hartl, A. Bracher, M. Hayer-Hartl
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