Microsecond Folding Dynamics of Apomyoglobin at Acidic pH
نویسندگان
چکیده
منابع مشابه
Sub-microsecond protein folding.
We have investigated the structure, equilibria, and folding kinetics of an engineered 35-residue subdomain of the chicken villin headpiece, an ultrafast-folding protein. Substitution of two buried lysine residues by norleucine residues stabilizes the protein by 1 kcal/mol and increases the folding rate sixfold, as measured by nanosecond laser T-jump. The folding rate at 300 K is (0.7 micros)(-1...
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How polypeptide chains acquire specific conformations to realize unique biological functions is a central problem of protein science. Single-molecule spectroscopy, combined with fluorescence resonance energy transfer, is utilized to study the conformational heterogeneity and the state-to-state transition dynamics of proteins on the submillisecond to second timescales. However, observation of th...
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ژورنال
عنوان ژورنال: The Journal of Physical Chemistry B
سال: 2012
ISSN: 1520-6106,1520-5207
DOI: 10.1021/jp3012365