Identification of a new site of conformational heterogeneity in unfolded ribonuclease A
dc.contributor.author | Adler, Marc | en_US |
dc.contributor.author | Scheraga, Harold A. | en_US |
dc.date.accessioned | 2006-09-11T15:39:28Z | |
dc.date.available | 2006-09-11T15:39:28Z | |
dc.date.issued | 1990-10 | en_US |
dc.identifier.citation | Adler, Marc; Scheraga, Harold A.; (1990). "Identification of a new site of conformational heterogeneity in unfolded ribonuclease A." Journal of Protein Chemistry 9(5): 583-588. <http://hdl.handle.net/2027.42/45087> | en_US |
dc.identifier.issn | 0277-8033 | en_US |
dc.identifier.issn | 1573-4943 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/45087 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=1964787&dopt=citation | en_US |
dc.description.abstract | The results presented here indicate that there are two slowly exchanging conformational isomers in unfolded bovine pancreatic ribonuclease A (RNase A) in the vicinity of Lys-41. The conformational heterogeneity is not observed in the fully folded protein. Therefore, one of the isomers may correspond to one of the slow-folding forms of the protein observed when refolding is initiated. These results were obtained from a chemically modified form of the protein, CL(7–41) RNase A, that has a dinitrophenyl cross-link between the ɛ-amino groups of Lys-7 and Lys-41. Extensive physical studies have shown that the cross-link does not significantly perturb the structure or the folding pathways of the protein. Therefore, the results obtained from this modified form of the protein are relevant to intact RNase A. The one-dimensional (1D) NMR spectrum of heat-unfolded CL(7–41) RNase A reveals that the singlet resonance for the C 3 H ring proton of the dinitrophenyl cross-link has been split into two unequal peaks in a 3:1 ratio, indicating that there are two distinct environments for the dinitrophenyl group. Variations in temperature, and the addition of urea, do not affect the relative peak intensities. The two peaks collapse into one after the protein is refolded. The observed splitting must originate from a slow reversible isomerization (>100 msec) in a neighboring bond. The two most likely candidates are either the cis/trans isomerization of the Lys-41-Pro-42 peptide bond or hindered rotation about the disulfide bond between Cys-40 and Cys-95. | en_US |
dc.format.extent | 546163 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers-Plenum Publishers; Plenum Publishing Corporation ; Springer Science+Business Media | en_US |
dc.subject.other | Protein Refolding | en_US |
dc.subject.other | Organic Chemistry | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Bioorganic Chemistry | en_US |
dc.subject.other | Animal Anatomy / Morphology / Histology | en_US |
dc.subject.other | RNase A | en_US |
dc.subject.other | Multiple Isomers | en_US |
dc.title | Identification of a new site of conformational heterogeneity in unfolded ribonuclease A | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Baker Laboratory of Chemistry, Cornell University, 14853-1301, Ithaca, New York; Biophysics Research Division, Institute of Science and Technology, University of Michigan, 48109, Ann Arbor, Michigan | en_US |
dc.contributor.affiliationother | Baker Laboratory of Chemistry, Cornell University, 14853-1301, Ithaca, New York | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 1964787 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/45087/1/10930_2005_Article_BF01025011.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1007/BF01025011 | en_US |
dc.identifier.source | Journal of Protein Chemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.