DC Field | Value | Language |
---|---|---|
dc.contributor.author | Dumont, Charles | ko |
dc.contributor.author | Matsumura, Yoshitaka | ko |
dc.contributor.author | Kim, Seung Joong | ko |
dc.contributor.author | Li, Jinsong | ko |
dc.contributor.author | Kondrashkina, Elena | ko |
dc.contributor.author | Kihara, Hiroshi | ko |
dc.contributor.author | Gruebele, Martin | ko |
dc.date.accessioned | 2018-10-19T00:43:39Z | - |
dc.date.available | 2018-10-19T00:43:39Z | - |
dc.date.created | 2018-10-01 | - |
dc.date.created | 2018-10-01 | - |
dc.date.issued | 2006-11 | - |
dc.identifier.citation | PROTEIN SCIENCE, v.15, no.11, pp.2596 - 2604 | - |
dc.identifier.issn | 0961-8368 | - |
dc.identifier.uri | http://hdl.handle.net/10203/246093 | - |
dc.description.abstract | The lambda(6-85)* pseudo-wild type of lambda repressor fragment is a fast two-state folder (k(f) approximate to 35 mu sec(-1) at 58 degrees C). Previously, highly stable lambda(6-85)* mutants with k(f) > 30 mu sec(-1) have been engineered to fold nearly or fully downhill. Stabilization of the native state by solvent tuning might also tune lambda(6-85)* away from two-state folding. We test this prediction by examining the folding thermodynamics and kinetics of lambda(6-85)* in a stabilizing solvent, 45% by weight aqueous ethylene glycol at -28 degrees C. Detection of kinetics by circular dichroism at 222 nm (sensitive to helix content) and small angle X-ray scattering (measuring the radius of gyration) shows that refolding from guanidine hydrochloride denatured conditions exhibits very different time scales for collapse and secondary structure formation: the two processes become decoupled. Collapse remains a low-barrier activated process, while the fastest of several secondary structure formation time scales approaches the downhill folding limit. Two-state folding of lambda(6-85)* is not a robust process. | - |
dc.language | English | - |
dc.publisher | COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT | - |
dc.subject | MONOMERIC LAMBDA-REPRESSOR | - |
dc.subject | FLOW CIRCULAR-DICHROISM | - |
dc.subject | FOLDING SPEED LIMIT | - |
dc.subject | X-RAY-SCATTERING | - |
dc.subject | BETA-LACTOGLOBULIN | - |
dc.subject | ABSORPTION-SPECTROSCOPY | - |
dc.subject | VISCOSITY DEPENDENCE | - |
dc.subject | SMALL PROTEINS | - |
dc.subject | KINETICS | - |
dc.subject | DOWNHILL | - |
dc.title | Solvent-tuning the collapse and helix formation time scales of lambda(*)(6-85) | - |
dc.type | Article | - |
dc.identifier.wosid | 000241666600014 | - |
dc.identifier.scopusid | 2-s2.0-33751071378 | - |
dc.type.rims | ART | - |
dc.citation.volume | 15 | - |
dc.citation.issue | 11 | - |
dc.citation.beginningpage | 2596 | - |
dc.citation.endingpage | 2604 | - |
dc.citation.publicationname | PROTEIN SCIENCE | - |
dc.identifier.doi | 10.1110/ps.062257406 | - |
dc.contributor.localauthor | Kim, Seung Joong | - |
dc.contributor.nonIdAuthor | Dumont, Charles | - |
dc.contributor.nonIdAuthor | Matsumura, Yoshitaka | - |
dc.contributor.nonIdAuthor | Li, Jinsong | - |
dc.contributor.nonIdAuthor | Kondrashkina, Elena | - |
dc.contributor.nonIdAuthor | Kihara, Hiroshi | - |
dc.contributor.nonIdAuthor | Gruebele, Martin | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | collapse | - |
dc.subject.keywordAuthor | heterogeneous kinetics | - |
dc.subject.keywordAuthor | cryosolvent | - |
dc.subject.keywordAuthor | stopped flow | - |
dc.subject.keywordPlus | MONOMERIC LAMBDA-REPRESSOR | - |
dc.subject.keywordPlus | FLOW CIRCULAR-DICHROISM | - |
dc.subject.keywordPlus | FOLDING SPEED LIMIT | - |
dc.subject.keywordPlus | X-RAY-SCATTERING | - |
dc.subject.keywordPlus | BETA-LACTOGLOBULIN | - |
dc.subject.keywordPlus | ABSORPTION-SPECTROSCOPY | - |
dc.subject.keywordPlus | VISCOSITY DEPENDENCE | - |
dc.subject.keywordPlus | SMALL PROTEINS | - |
dc.subject.keywordPlus | KINETICS | - |
dc.subject.keywordPlus | DOWNHILL | - |
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