Biphasic reductive unfolding of ribonuclease A is temperature dependent.
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Summary
The kinetics of the reversible thermal unfolding, irreversible Thermal unfolding, and reductive unfolding processes of bovine pancreatic ribonuclease A (RNase A) were investigated in NaCl/Pi solutions.
- Type
- article
- Published
- 2002-11-01
- Cited by
- 21
- References
- 29
- Access
- Open access
- OpenAlex
- https://openalex.org/W1590694048
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:41466514
Keywords
Bovine pancreatic ribonuclease, Dithiothreitol, Chemistry, Reagent, RNase P
References
- On the Thermal Unfolding Character of Globular Proteins
- Effects of pH on the kinetic reaction
- Charge density-dependent strength of hydration and biological structure.
- Acceleration of oxidative folding of bovine pancreatic ribonuclease A by anion‐induced stabilization and formation of structured native‐like intermediates
- 15N backbone dynamics of the S‐peptide from ribonuclease A in its free and S‐protein bound forms: Toward a site‐specific analysis of entropy changes upon folding
- Steps in the pathway of the thermal unfolding of ribonuclease A. A nonspecific photochemical surface-labeling study.
- Thermodynamic stability of ribonuclease A in alkylurea solutions and preferential solvation changes accompanying its thermal denaturation: A calorimetric and spectroscopic study
- Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A.
- Mechanism of reductive protein unfolding
- Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.
- Regeneration of bovine pancreatic ribonuclease A. 4. Temperature dependence of the regeneration rate.
- Regeneration of bovine pancreatic ribonuclease A. 3. Dependence on the nature of the redox reagent.
- Regeneration of bovine pancreatic ribonuclease A. 1. Steady-state distribution.
- Two new structured intermediates in the oxidative folding of RNase A
- Regeneration of bovine pancreatic ribonuclease A: detailed kinetic analysis of two independent folding pathways.
- Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy.
- Regeneration of bovine pancreatic ribonuclease A: identification of two nativelike three-disulfide intermediates involved in separate pathways.
- Two-state kinetics characterized by image analysis of nuclear magnetic resonance spectra
- Structural characterization of a three-disulfide intermediate of ribonuclease A involved in both the folding and unfolding pathways.
- Regeneration of bovine pancreatic ribonuclease A. 2. Kinetics of regeneration.
Cited by
- Hemoglobin senses body temperature
- Oligomerization of ribonuclease A under reducing conditions.
- Two-dimensional infrared correlation spectroscopy study of sequential events in the heat-induced unfolding and aggregation process of myoglobin.
- Improvement of “concatenated” two-dimensional correlation analysis and its new potential applications on the quantitative evaluation of the process reversibility under different perturbations
- Protein thermal aggregation involves distinct regions: sequential events in the heat-induced unfolding and aggregation of hemoglobin.
- Concatenated Two-Dimensional Correlation Analysis: A New Possibility for Generalized Two-Dimensional Correlation Spectroscopy and its Application to the Examination of Process Reversibility
- Effects of spermine NONOate and ATP on protein aggregation: light scattering evidences
- On the thermal stability of the two dimeric forms of ribonuclease A.
- The N-terminus modulates human Caf1 activity, structural stability and aggregation.
- Structural transition temperature of hemoglobins correlates with species’ body temperature
- A principal component analysis and two-dimensional correlation infrared spectroscopy study on the thermal unfolding of ribonuclease A under reducing conditions
- Thermally induced early events of ribonuclease A under reducing conditions: Evidenced by principal component analysis and two-dimensional correlation infrared spectroscopy
- Oxidative folding and N-terminal cyclization of onconase.
- Body temperature-related structural transitions of monotremal and human hemoglobin.
- Oxidative folding of hirudin in human serum.
- Phase diagram of androsterol-dipalmitoylphosphatidylcholine mixtures dispersed in excess water.
- Regional cooperativity in the phase transitions of dipalmitoylphosphatidylcholine bilayers: the lipid tail triggers the isothermal crystallization process.
- Dissimilarity in the reductive unfolding pathways of two ribonuclease homologues.
- The role of sterol rings and side chain on the structure and phase behaviour of sphingomyelin bilayers
- Characteristics of type IV collagen unfolding under various pH conditions as a model of pathological disorder in tissue.
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