Conformational stability and mechanism of folding of ribonuclease T1
نویسندگان
چکیده
منابع مشابه
Protein Stability, Folding, Disaggregation and Etiology of Conformational Malfunctions
Estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. Today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. A...
متن کاملConformational stability of ribonuclease T1 determined by hydrogen-deuterium exchange.
The hydrogen-deuterium exchange kinetics of 37 backbone amide residues in RNase T1 have been monitored at 25, 40, 45, and 50 degrees C at pD 5.6 and at 40 and 45 degrees C at pD 6.6. The hydrogen exchange rate constants of the hydrogen-bonded residues varied over eight orders of magnitude at 25 degrees C with 13 residues showing exchange rates consistent with exchange occurring as a result of g...
متن کاملprotein stability, folding, disaggregation and etiology of conformational malfunctions
estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. a...
متن کاملContribution of histidine residues to the conformational stability of ribonuclease T1 and mutant Glu-58----Ala.
The pK values of the histidine residues in ribonuclease T1 (RNase T1) are unusually high: 7.8 (His-92), 7.9 (His-40), and 7.3 (His-27) [Inagaki et al. (1981) J. Biochem. 89, 1185-1195]. In the RNase T1 mutant Glu-58----Ala, the first two pK values are reduced to 7.4 (His-92) and 7.1 (His-40). These lower pKs were expected since His-92 (5.5 A) and His-40 (3.7 A) are in close proximity to Glu-58 ...
متن کاملAre turns required for the folding of ribonuclease T1?
Ribonuclease T1 (RNase T1) is a small, globular protein of 104 amino acids for which extensive thermodynamic and structural information is known. To assess the specific influence of variations in amino acid sequence on the mechanism for protein folding, circularly permuted variants of RNase T1 were constructed and characterized in terms of catalytic activity and thermodynamic stability. The dis...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)80107-7