Vibrational circular dichroism study of polypeptide model-membrane systems
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F12%3A43893351" target="_blank" >RIV/60461373:22340/12:43893351 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.ab.2012.03.023" target="_blank" >http://dx.doi.org/10.1016/j.ab.2012.03.023</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.ab.2012.03.023" target="_blank" >10.1016/j.ab.2012.03.023</a>
Alternative languages
Result language
angličtina
Original language name
Vibrational circular dichroism study of polypeptide model-membrane systems
Original language description
In this article, we describe the mutual structural effect of the interaction between the model membranes and polylysine and poly-L-arginine. Vibrational circular dichroism (VCD), a method exceptionally sensitive to the polypeptide structure that has notbeen established in such studies before, was the primary method of this study. A complementary technique, electronic circular dichroism, was applied to verify the newly obtained results and as a bridge to the previous studies. We used micelles composed of sodium dodecyl sulfate (SDS) as a monolayer membrane model and large unilamellar vesicles composed of phospholipids as a bilayer membrane model. We describe the conformational changes of the polypeptides caused by the interaction with the model membranes. Among others, the presence of the liposomes in the solution generated special conditions for the formation of the alpha-helical structure of poly-L-arginine; the presence of SDS induced the formation of the beta-structure of polylysin
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CB - Analytical chemistry, separation
OECD FORD branch
—
Result continuities
Project
—
Continuities
S - Specificky vyzkum na vysokych skolach
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
Analytical Biochemistry
ISSN
0003-2697
e-ISSN
—
Volume of the periodical
427
Issue of the periodical within the volume
2
Country of publishing house
US - UNITED STATES
Number of pages
8
Pages from-to
211-218
UT code for WoS article
000306872200019
EID of the result in the Scopus database
—