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Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy

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TitleInfo
Title
Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy
Name (type = personal)
NamePart (type = family)
Talaga
NamePart (type = given)
David S.
Role
RoleTerm (authority = marcrt); (type = text)
author
Name (type = personal)
NamePart (type = family)
Lau
NamePart (type = given)
Wai Leung
Role
RoleTerm (authority = marcrt); (type = text)
author
Name (type = personal)
NamePart (type = family)
Roder
NamePart (type = given)
Heinrich
Role
RoleTerm (authority = marcrt); (type = text)
author
Name (type = personal)
NamePart (type = family)
Tang
NamePart (type = given)
Jianyong
Role
RoleTerm (authority = marcrt); (type = text)
author
Name (type = personal)
NamePart (type = family)
Jia
NamePart (type = given)
Yiwei
Role
RoleTerm (authority = marcrt); (type = text)
author
Name (type = personal)
NamePart (type = family)
DeGrado
NamePart (type = given)
William F.
Role
RoleTerm (authority = marcrt); (type = text)
author
Name (type = personal)
NamePart (type = family)
Hochstrasser
NamePart (type = given)
Robin M.
Role
RoleTerm (authority = marcrt); (type = text)
author
Name (type = corporate)
NamePart
National Institutes of Health
Role
RoleTerm (authority = marcRelator)
funder
Name (authority = RutgersOrg-Department); (type = corporate)
NamePart
Chemistry & Chemical Biology
Name (authority = RutgersOrg-School); (type = corporate)
NamePart
School of Arts and Sciences (SAS) (New Brunswick)
TypeOfResource
Text
Genre (authority = RULIB-FS)
Article, Refereed
Genre (authority = NISO JAV)
Accepted Manuscript (AM)
OriginInfo
DateCreated (encoding = w3cdtf); (keyDate = yes); (qualifier = exact)
2000
Publisher
National Academy of Sciences
Language
LanguageTerm
English
PhysicalDescription
Form (authority = RULIB)
manuscript
InternetMediaType
application/pdf
Extent
6 pages
Abstract
We report single-molecule measurements on the folding and unfolding conformational equilibrium distributions and dynamics of a disulfide crosslinked version of the two-stranded coiled coil from GCN4. The peptide has a fluorescent donor and acceptor at the N termini of its two chains and a Cys disulfide near its C terminus. Thus, folding brings the two N termini of the two chains close together, resulting in an enhancement of fluorescent resonant energy transfer. End-to-end distance distributions have thus been characterized under conditions where the peptide is nearly fully folded (0 M urea), unfolded (7.4 M urea), and in dynamic exchange between folded and unfolded states (3.0 M urea). The distributions have been compared for the peptide freely diffusing in solution and deposited onto aminopropyl silanized glass. As the urea concentration is increased, the mean end-to-end distance shifts to longer distances both in free solution and on the modified surface. The widths of these distributions indicate that the molecules are undergoing millisecond conformational fluctuations. Under all three conditions, these fluctuations gave nonexponential correlations on 1- to 100-ms time scale. A component of the correlation decay that was sensitive to the concentration of urea corresponded to that measured by bulk relaxation kinetics. Thetrajectories provided effective intramolecular diffusion coefficients as a function of the end-to-end distances for the folded and unfolded states. Single-molecule folding studies provide information concerning the distributions of conformational states in the folded, unfolded, and dynamically interconverting states.
Note (type = citation)
Author manuscript. Published in final edited form as: Proc Natl Acad Sci U S A. 2000 November 21; 97(24): 13021-13026.
Note (type = publisherStatement)
The final published version of this article is located at: http://www.pnas.org/cgi/reprint/97/24/13021
Note (type = grantNumber)
NIH GM54616; to William F. DeGrado
Note
NIH GM12592; to Robin M. Hochstrasser
Note
NIH GM48130; to William F. Degrado and Robin M. Hochstrasser
Note
This work was supported by GM54616 (to W.F.D.), GM12592 (to R.M.H.) and GM48130 (to W.F.D. and R.M.H.) with instrumentation developed under RR01348. D.S.T. was supported by National Institutes of Health Grant NRSA F32-GM18589.
Note
Also available in PubMed Central. PMCID:PMC27171
Subject (authority = Other)
Topic
Peptides
RelatedItem (type = host)
TitleInfo
Title
Talaga, David
Identifier (type = local)
rucore00000001072
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore00000001072.Article.16091
Identifier (type = FEDORA_PID)
rutgers-lib:23073
Identifier (type = doi)
doi:10.7282/T3Q81BD8
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Extension
DescriptiveEvent
Type
Citation
DateTime (encoding = w3cdtf)
2000
AssociatedObject
Type
Journal
Relationship
Has part
Name
Proceedings of the National Academy of Sciences of the United States of America
Identifier (type = volume and issue)
97(24)
Reference (type = digital)
http://dx.doi.org/10.1073/pnas.97.24.13021
Detail
13021-13026
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Copyright for scholarly resources published in RUcore is retained by the copyright holder. By virtue of its appearance in this open access medium, you are free to use this resource, with proper attribution, in educational and other non-commercial settings. Other uses, such as reproduction or republication, may require the permission of the copyright holder.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
RightsHolder (ID = 1)
Name (TYPE = corporate)
CorporateName
National Academy of Sciences
RightsEvent (AUTHORITY = rulib); (ID = 1)
Type
Permission or license
AssociatedEntity (AUTHORITY = rulib); (ID = 1)
Name
David Talaga
Role
Donor
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I hereby grant to Rutgers, The State University of New Jersey (Rutgers) the non-exclusive right to retain, reproduce, and distribute the deposited work (Work) in whole or in part, in and from its electronic format, without fee. This agreement does not represent a transfer of copyright to Rutgers. Rutgers may make and keep more than one copy of the Work for purposes of security, backup, preservation, and access and may migrate the Work to any medium or format for the purpose of preservation and access in the future. Rutgers will not make any alteration, other than as allowed by this agreement, to the Work. I represent and warrant to Rutgers that the Work is my original work. I also represent that the Work does not, to the best of my knowledge, infringe or violate any rights of others. I further represent and warrant that I have obtained all necessary rights to permit Rutgers to reproduce and distribute the Work and that any third-party owned content is clearly identified and acknowledged within the Work. By granting this license, I acknowledge that I have read and agreed to the terms of this agreement and all related RUcore and Rutgers policies.
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