Energetics of ribonuclease T1 structure

The energetics of thermal denaturation of two isoforms of ribonuclease T1 (Gln25 and Lys25) in various solvents have been studied by differential scanning calorimetry. It has been shown that the thermal transition of both forms of RNase T1 is strongly affected by slow kinetics, which cause an appare...

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Bibliographic Details
Published in:Biochemistry (Easton) 1994-03, Vol.33 (11), p.3312-3319
Main Authors: Yu, Yihua, Makhatadze, George I, Pace, C. Nick, Privalov, Peter L
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
ASPERGILLUS ORYZAE
Aspergillus oryzae - enzymology
Biological and medical sciences
Calorimetry, Differential Scanning
Chemical Phenomena
Chemistry, Physical
DEGRADACION
DEGRADATION
ENERGIA
ENERGIE
Enzyme Stability
Enzymes and enzyme inhibitors
Escherichia coli
FISICA
Fundamental and applied biological sciences. Psychology
HIDROGENO
Hot Temperature
Hydrogen Bonding
HYDROGENE
Hydrolases
Kinetics
PHYSIQUE
PROPIEDADES TERMICAS
PROPRIETE THERMIQUE
Protein Denaturation
Recombinant Proteins - chemistry
RIBONUCLEASAS
RIBONUCLEASE
Ribonuclease T1 - chemistry
Thermodynamics
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Summary:The energetics of thermal denaturation of two isoforms of ribonuclease T1 (Gln25 and Lys25) in various solvents have been studied by differential scanning calorimetry. It has been shown that the thermal transition of both forms of RNase T1 is strongly affected by slow kinetics, which cause an apparent deviation of the transition from a simple two-state model. By decreasing the heating rate or increasing the transition temperature, the denaturation of RNase approaches an equilibrium two-state transition. This permits determination of the thermodynamic parameters characterizing unfolding of the native structure. These thermodynamic parameters were correlated with the structural features of protein. Analysis of different contributions to the stability of RNase T1 shows that van der Waals interactions and hydrogen bonding are the major contributors to the conformational stability of the protein
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00177a023