Abolition of the fast track of lysozyme folding at neutral pH

Studies in this laboratory have shown nat [he reLozolng of lysozyme is accelerated in the presence of equimolar GroEL. We are now investigating the molecular origin of this rate enchancement. The conditions under which the rate enhancement occurs are pH 7.2, 400 mM KCI, and GroEL. The first step in...

Full description

Bibliographic Details
Main Authors: Texter, F, Coyle, J, Kulkarni, S, Robinson, C, Radford, SE
Format: Journal article
Language:English
Published: 1997
_version_ 1797081016613994496
author Texter, F
Coyle, J
Kulkarni, S
Robinson, C
Radford, SE
author_facet Texter, F
Coyle, J
Kulkarni, S
Robinson, C
Radford, SE
author_sort Texter, F
collection OXFORD
description Studies in this laboratory have shown nat [he reLozolng of lysozyme is accelerated in the presence of equimolar GroEL. We are now investigating the molecular origin of this rate enchancement. The conditions under which the rate enhancement occurs are pH 7.2, 400 mM KCI, and GroEL. The first step in this study is a reexamination of the folding mechanism of lysozyme under these conditions in the absence of GroEL. Here we present the folding pathway of ivsozvme under these conditions determined using fluorescence, circular dichroism, hydrogen exchange labeling. IH-NMR, and electrospray ionization mass spectrometry (ESI-MS). We show that under these conditions the fast track folding is no longer populated, but that folding still occurs along parallel pathways. (This work was carried out while FLT was on sabbatical leave at te Universities of Oxford and Leeds, supported by an Albright College Sabbatical Grant. The work was supported by grants from BBSRC, MRS, The Roya] Society and The Wellcome Trust.).
first_indexed 2024-03-07T01:08:33Z
format Journal article
id oxford-uuid:8c2d4ddc-ccea-41a5-8f22-c63a643618b3
institution University of Oxford
language English
last_indexed 2024-03-07T01:08:33Z
publishDate 1997
record_format dspace
spelling oxford-uuid:8c2d4ddc-ccea-41a5-8f22-c63a643618b32022-03-26T22:43:00ZAbolition of the fast track of lysozyme folding at neutral pHJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:8c2d4ddc-ccea-41a5-8f22-c63a643618b3EnglishSymplectic Elements at Oxford1997Texter, FCoyle, JKulkarni, SRobinson, CRadford, SEStudies in this laboratory have shown nat [he reLozolng of lysozyme is accelerated in the presence of equimolar GroEL. We are now investigating the molecular origin of this rate enchancement. The conditions under which the rate enhancement occurs are pH 7.2, 400 mM KCI, and GroEL. The first step in this study is a reexamination of the folding mechanism of lysozyme under these conditions in the absence of GroEL. Here we present the folding pathway of ivsozvme under these conditions determined using fluorescence, circular dichroism, hydrogen exchange labeling. IH-NMR, and electrospray ionization mass spectrometry (ESI-MS). We show that under these conditions the fast track folding is no longer populated, but that folding still occurs along parallel pathways. (This work was carried out while FLT was on sabbatical leave at te Universities of Oxford and Leeds, supported by an Albright College Sabbatical Grant. The work was supported by grants from BBSRC, MRS, The Roya] Society and The Wellcome Trust.).
spellingShingle Texter, F
Coyle, J
Kulkarni, S
Robinson, C
Radford, SE
Abolition of the fast track of lysozyme folding at neutral pH
title Abolition of the fast track of lysozyme folding at neutral pH
title_full Abolition of the fast track of lysozyme folding at neutral pH
title_fullStr Abolition of the fast track of lysozyme folding at neutral pH
title_full_unstemmed Abolition of the fast track of lysozyme folding at neutral pH
title_short Abolition of the fast track of lysozyme folding at neutral pH
title_sort abolition of the fast track of lysozyme folding at neutral ph
work_keys_str_mv AT texterf abolitionofthefasttrackoflysozymefoldingatneutralph
AT coylej abolitionofthefasttrackoflysozymefoldingatneutralph
AT kulkarnis abolitionofthefasttrackoflysozymefoldingatneutralph
AT robinsonc abolitionofthefasttrackoflysozymefoldingatneutralph
AT radfordse abolitionofthefasttrackoflysozymefoldingatneutralph