Correlation of folding kinetics with the number and isomerization states of prolines in three homologous proteins of the RNase family
DC Field | Value | Language |
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dc.contributor.author | Pradeep, Lovy | - |
dc.contributor.author | Shin, Hang-Cheol | - |
dc.contributor.author | Scheraga, Harold A. | - |
dc.date.available | 2018-05-10T17:09:00Z | - |
dc.date.created | 2018-04-17 | - |
dc.date.issued | 2006-09-18 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/18600 | - |
dc.description.abstract | Several studies attribute the slower phases in protein folding to prolyl isomerizations, and several others do not. A correlation exists between the number of prolines in a protein and the complexity of the mechanism with which it folds. In this study, we have demonstrated a direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds via slower phases by studying the folding of three structurally homologous proteins of the ribonuclease family, namely RNase A, onconase and angiogenin, which differ in the number and isomerization states of their proline residues. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.relation.isPartOf | FEBS LETTERS | - |
dc.subject | PANCREATIC RIBONUCLEASE-A | - |
dc.subject | MAGNETIC-RESONANCE SPECTROSCOPY | - |
dc.subject | CIS-TRANS ISOMERIZATION | - |
dc.subject | STAPHYLOCOCCAL NUCLEASE | - |
dc.subject | BOVINE ANGIOGENIN | - |
dc.subject | UNFOLDED STATE | - |
dc.subject | MUTATIONS | - |
dc.subject | RESIDUES | - |
dc.subject | STABILITY | - |
dc.subject | ISOMERISM | - |
dc.title | Correlation of folding kinetics with the number and isomerization states of prolines in three homologous proteins of the RNase family | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.febslet.2006.08.024 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | FEBS LETTERS, v.580, no.21, pp.5029 - 5032 | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000240693200009 | - |
dc.identifier.scopusid | 2-s2.0-33748286745 | - |
dc.citation.endPage | 5032 | - |
dc.citation.number | 21 | - |
dc.citation.startPage | 5029 | - |
dc.citation.title | FEBS LETTERS | - |
dc.citation.volume | 580 | - |
dc.contributor.affiliatedAuthor | Shin, Hang-Cheol | - |
dc.type.docType | Article | - |
dc.description.oadoiVersion | published | - |
dc.subject.keywordAuthor | protein folding | - |
dc.subject.keywordAuthor | proline isomerization | - |
dc.subject.keywordAuthor | ribonuclease family | - |
dc.subject.keywordAuthor | structurally homologous proteins | - |
dc.subject.keywordAuthor | folding kinetics | - |
dc.subject.keywordAuthor | conformational folding | - |
dc.subject.keywordPlus | PANCREATIC RIBONUCLEASE-A | - |
dc.subject.keywordPlus | MAGNETIC-RESONANCE SPECTROSCOPY | - |
dc.subject.keywordPlus | CIS-TRANS ISOMERIZATION | - |
dc.subject.keywordPlus | STAPHYLOCOCCAL NUCLEASE | - |
dc.subject.keywordPlus | BOVINE ANGIOGENIN | - |
dc.subject.keywordPlus | UNFOLDED STATE | - |
dc.subject.keywordPlus | MUTATIONS | - |
dc.subject.keywordPlus | RESIDUES | - |
dc.subject.keywordPlus | STABILITY | - |
dc.subject.keywordPlus | ISOMERISM | - |
dc.description.journalRegisteredClass | scopus | - |
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