Role of different beta-turns in beta-hairpin conformation and stability studied by optical spectroscopy
Identifikátory výsledku
Kód výsledku v 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>
Výsledek na webu
<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>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Role of different beta-turns in beta-hairpin conformation and stability studied by optical spectroscopy
Popis výsledku v původním jazyce
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
Název v anglickém jazyce
Role of different beta-turns in beta-hairpin conformation and stability studied by optical spectroscopy
Popis výsledku anglicky
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
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CE - Biochemie
OECD FORD obor
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Návaznosti výsledku
Projekt
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Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2012
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Proteins: Structure, Function, and Bioinformatics
ISSN
1097-0134
e-ISSN
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Svazek periodika
80
Číslo periodika v rámci svazku
1
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
7
Strana od-do
44-60
Kód UT WoS článku
000298598800005
EID výsledku v databázi Scopus
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