Title data
Hagerman, Paul J. ; Schmid, Franz X. ; Baldwin, Robert L.:
Refolding behavior of a kinetic intermediate observed in the low pH unfolding of ribonuclease A.
In: Biochemistry.
Vol. 18
(1979)
Issue 2
.
- pp. 293-297.
ISSN 1520-4995
DOI: https://doi.org/10.1021/bi00569a009
Related URLs
Abstract in another language
A transient intermediate (I3) observed previously in the unfolding of ribonuclease A has been studied by employing a sequential mixing instrument to populate selectively this species. This approach has made it possible both to determine the refolding behavior of this species and to characterize further the kinetics of its formation. (1) Formation of I3 represents the earliest detectable change in unfolding. (2) The loss of the 2'CMP binding site occurs in parallel with the exposure of the interior of the protein to solvent. (3) I3 is distinct from previously described intermediates in refolding. (4) Overall condensation of the protein to exclude solvent from the interior, as well as the formation of a substrate binding site, takes place in approximately 30 ms (pH 5.8, 47 degrees C), indicating that the formation of native structure can take place faster than had previously been supposed.
Further data
Item Type: | Article in a journal |
---|---|
Refereed: | Yes |
Additional notes: | PubMed-ID: 33695 |
Institutions of the University: | Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professor Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors |
Result of work at the UBT: | No |
DDC Subjects: | 500 Science > 540 Chemistry |
Date Deposited: | 29 Apr 2015 13:48 |
Last Modified: | 20 Apr 2022 12:30 |
URI: | https://eref.uni-bayreuth.de/id/eprint/11219 |