Protein stability: electrostatics and compact denatured states.
نویسندگان
چکیده
منابع مشابه
Thermodynamics of protein denatured states.
Recent work on the thermodynamics of protein denatured states is providing insight into the stability of residual structure and the conformational constraints that affect the disordered states of proteins. Current data from native state hydrogen exchange and the pH dependence of protein stability indicate that residual structure can modulate the stability of the denatured state by up to 4 kcal ...
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Fluorescence and circular dichroism stopped-flow have been widely used to determine the kinetics of protein folding including folding rates and possible folding pathways. Yet, these measurements are not able to provide spatial information of protein folding/unfolding. Especially, conformations of denatured states cannot be elaborated in detail. In this study, we apply the method of fluorescence...
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The presence of a solvent-exposed alanine residue stabilizes a helix by 0.4-2 kcal.mol(-1) relative to glycine. Various factors have been suggested to account for the differences in helical propensity, from the higher conformational freedom of glycine sequences in the unfolded state to hydrophobic and van der Waals' stabilization of the alanine side chain in the helical state. We have performed...
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Amyloid fibril formation and deposition have been associated with a series of diseases, including Alzheimer ́s, Spongiform encephalopathies, and several systemic amyloidosis. In most of these amyloid diseases, it has been shown that the normal precursor protein, due to proteolysis, mutation or molecular environment stress, undergoes misfolding, leading to molecular species with a high tendency f...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1991
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.88.10.4176