Downhill, Ultrafast and Fast Folding Proteins Revised
نویسندگان
چکیده
منابع مشابه
Fast protein folding on downhill energy landscape.
Proteins fold in a time range of microseconds to minutes despite the large amount of possible conformers. Molecular dynamics simulations of a three-stranded antiparallel beta-sheet peptide (for a total of 12.6 microsec and 72 folding events) show that at the melting temperature the unfolded state ensemble contains many more conformers than those sampled during a folding event.
متن کاملOsmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization
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...
متن کاملOsmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization
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...
متن کاملAnalysis of ‘downhill’ protein folding
There is controversy as to whether homologues from the peripheral subunit binding domain family of small proteins fold ‘downhill’ (that is, non-cooperatively, in the absence of free-energy barriers between conformations) and whether they modulate their size for biological function. Sadqi et al. claim that Naf-BBL — a naphthylalaninelabelled, truncated version of this domain — folds in this way,...
متن کاملRobustness of downhill folding: guidelines for the analysis of equilibrium folding experiments on small proteins.
Previously, we identified the protein BBL as a downhill folder. This conclusion was based on the statistical mechanical analysis of equilibrium experiments performed in two variants of BBL, one with a fluorescent label at the N-terminus, and another one labeled at both ends. A recent report has claimed that our results are an artifact of label-induced aggregation and that BBL with no fluorescen...
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ژورنال
عنوان ژورنال: International Journal of Molecular Sciences
سال: 2020
ISSN: 1422-0067
DOI: 10.3390/ijms21207632