Searching for "downhill scenarios" in protein folding
نویسندگان
چکیده
منابع مشابه
Commentary Searching for ‘‘downhill scenarios’’ in protein folding
The genome project, with the discovery of thousands of new protein sequences every year, has created a revolution in protein physics, chemistry, and biology. This has led to a renewed and very much expanded interest in the protein folding problem, particularly among biophysical scientists. There are two parts to this problem. The first is predicting the three-dimensional structure of a protein ...
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,...
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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.
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Classical protein folding invokes a cooperative transition between distinct thermodynamic states that are individually populated at equilibrium and separated by an energy barrier. It has been proposed, however, that the small protein, BBL, undergoes one-step downhill folding whereby it folds non-cooperatively to its native state without encountering an appreciable energy barrier. Only a single ...
متن کاملExperimental identification of downhill protein folding.
Theory predicts the existence of barrierless protein folding. Without barriers, folding should be noncooperative and the degree of native structure should be coupled to overall protein stability. We investigated the thermal unfolding of the peripheral subunit binding domain from Escherichia coli's 2-oxoglutarate dehydrogenase multienzyme complex (termed BBL) with a combination of spectroscopic ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1999
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.96.11.5897