OXIDIZED RNASE AS A PROTEIN MODEL HAVING NO CONTRIBUTION TO THE HYDROGEN EXCHANGE RATE FROM CONFORMATIONAL RESTRICTIONS
- 1 August 1970
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 66 (4), 1067-1074
- https://doi.org/10.1073/pnas.66.4.1067
Abstract
As oxidized RNase is a model for the random conformation state of RNase, the hydrogen exchange kinetics of oxidized RNase approximate the intrinsic conformation-independent chemical exchange rate of the native protein. The energy of activation, the pH(min), and the k(min) of oxidized RNase exchange rates are similar to those reported for amino acid homopolymers. However, unlike the exchange from homopolymers, the exchange from oxidized RNase is characterized by a distribution of first-order rates. This distribution is important to the analysis of exchange from native proteins in terms of classes of sites which share common structural properties.Keywords
This publication has 20 references indexed in Scilit:
- Dimensions of protein random coilsBiochemistry, 1968
- Protein DenaturationAdvances in protein chemistry, 1968
- The Tritium-Hydrogen Exchange of Myosin and Its Proteolytic Fragments*Biochemistry, 1967
- Hydrogen Exchange in ProteinsAdvances in protein chemistry, 1966
- Structural Transformations of Bovine Pancreatic Ribonuclease in Solution: A Study of Polarization of FluorescenceJournal of Biological Chemistry, 1963
- Hydrogen-deuterium exchange of small peptides in aqueous solutionBiochimica et Biophysica Acta, 1960
- Difference spectra of ribonuclease and two ribonuclease derivatives.1960
- A comparison of the physical chemical properties of oxidized and reduced alkylated ribonucleaseBiochimica et Biophysica Acta, 1959
- THE REACTION OF O-METHYLISOUREA WITH BOVINE PANCREATIC RIBONUCLEASEJournal of Biological Chemistry, 1957
- EVIDENCE FOR THE INSTABILITY OF HYDROGEN-BONDED PEPTIDE STRUCTURES IN WATER, BASED ON STUDIES OF RIBONUCLEASE AND OXIDIZED RIBONUCLEASE1956