Thermally versus Chemically Denatured Protein States
نویسندگان
چکیده
منابع مشابه
Conformational entropy of alanine versus glycine in protein denatured states.
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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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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Thermally denatured chymotrypsin, lysozyme and papain are substantially refolded towards their native conformation by gold nanoparticle bearing dicarboxylate sidechains.
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Biosynthetic preparation and (19)F NMR experiments on uniformly 3-fluorotyrosine-labeled green fluorescent protein (GFP) are described. The (19)F NMR signals of all 10 fluorotyrosines are resolved in the protein spectrum with signals spread over 10 ppm. Each tyrosine in GFP was mutated in turn to phenylalanine. The spectra of the Tyr --> Phe mutants, in conjunction with relaxation data and resu...
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The noncovalent complex formed by the association of two fragments of chymotrypsin inhibitor-2 is reversibly denatured by pressure in the absence of chemical denaturants. On pressure release, the complex returned to its original conformation through a biphasic reaction, with first-order rate constants of 0.012 and 0.002 s-1, respectively. The slowest phase arises from an interconversion of the ...
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ژورنال
عنوان ژورنال: Biochemistry
سال: 2019
ISSN: 0006-2960,1520-4995
DOI: 10.1021/acs.biochem.9b00089