Identification and characterization of protein folding intermediates
نویسندگان
چکیده
منابع مشابه
Characterizing protein folding intermediates.
To determine the pathway by which a protein folds up, it is necessary to characterize the structures of folding intermediates and also to place these intermediates in the correct order on the kinetic pathway of folding. Noncovalent folding reactions are fast: typically they occur in seconds or less for small single-domain proteins. On the other hand, hours are required to obtain detailed struct...
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The folding reactions of some small proteins show clear evidence of a hierarchic process, whereas others, lacking detectable intermediates, do not. Evidence from folding intermediates and transition states suggests that folding begins locally, and that the formation of native secondary structure precedes the formation of tertiary interactions, not the reverse. Some notable examples in the liter...
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It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...
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It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...
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We have employed two-dimensional solid-state NMR to study structure and dynamics of insoluble folding states of the domain-swapped protein Crh. Starting from the protein precipitated at its pI, conformational changes due to a modest temperature increase were investigated at the level of individual residues and in real-time. As compared to the crystalline state, Crh pI-precipitates exhibited a h...
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ژورنال
عنوان ژورنال: Biophysical Chemistry
سال: 2007
ISSN: 0301-4622
DOI: 10.1016/j.bpc.2007.04.008