Linked Life Data

7947747

Source:http://linkedlifedata.com/resource/pubmed/id/7947747

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
45
pubmed:dateCreated
1994-12-19
pubmed:abstractText
We recently developed an experiment, termed continuous-flow quasielastic light scattering (QLS), that is capable of monitoring the time evolution of the hydrodynamic diameter of macromolecules or macromolecular assemblies in solution. Here we report the use of this method to directly monitor the kinetics of compaction of the polypeptide chain of hen egg white lysozyme (HEWL) when protein refolding is initiated by 10-fold dilution from 5 M guanidine hydrochloride (GuHCl) at pH 1.5, 23 degrees C. Previously, such information could only be obtained indirectly, by analysis of the kinetics of binding ans release of a fluorescent probe dye. Refolding was also monitored by UV difference absorption spectroscopy to characterize the time scale of the formation of the native environment around the aromatic side chains under the same conditions used in the continuous-flow QLS experiments. We find that HEWL becomes compact within 1 s after the initiation of refolding, the shortest time that is accessible with our first-generation instrument. This time scale is shorter than that for the recovery of the native absorbances in the aromatic region. These results provide direct evidence that the intermediate on the folding pathway of lysozyme is compact. The implications of these results for models of protein folding are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13382-90
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Kinetics of compaction during lysozyme refolding studied by continuous-flow quasielastic light scattering.
pubmed:affiliation
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.