Role of different beta-turns in beta-hairpin conformation and stability studied by optical spectroscopy
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F12%3A43893267" target="_blank" >RIV/60461373:22340/12:43893267 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1002/prot.23140" target="_blank" >http://dx.doi.org/10.1002/prot.23140</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/prot.23140" target="_blank" >10.1002/prot.23140</a>
Alternative languages
Result language
angličtina
Original language name
Role of different beta-turns in beta-hairpin conformation and stability studied by optical spectroscopy
Original language description
Model beta-hairpin peptides based on variations in the turn sequence of Cochran's tryptophan zipper peptide, SWTWENGKWTWK, were studied using electronic circular dichroism (ECD), fluorescence, and infrared (IR) spectroscopies. The trpzip2 AsnGly turn sequence was substituted with ThrGly, AibGly, DProGly, and GlyAsn (trpzip1) to study the impact of turn stability on beta-hairpin formation. Stability and conformational changes of these hairpins were monitored by thermodynamic analyses of the temperature variation of both FTIR (amide I') and ECD spectral intensities. These changes were fit to a two-state model which yielded different Tm values, representing the folding/unfolding process, for hairpins with different beta-turns. Different beta-turns show systematic contributions to hairpin structure formation, and their inclusion in hairpin design can modify the folding pathways. AibGly or DProGly sequences stabilize the turn resulting in residual TrpTrp interaction at high temperatures, bu
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proteins: Structure, Function, and Bioinformatics
ISSN
1097-0134
e-ISSN
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Volume of the periodical
80
Issue of the periodical within the volume
1
Country of publishing house
US - UNITED STATES
Number of pages
7
Pages from-to
44-60
UT code for WoS article
000298598800005
EID of the result in the Scopus database
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