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A Solid Phase Vibrational Circular Dichroism Study of Polypeptide-Surfactant Interaction

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F15%3A43900287" target="_blank" >RIV/60461373:22340/15:43900287 - isvavai.cz</a>

  • Result on the web

    <a href="http://onlinelibrary.wiley.com/doi/10.1002/chir.22534/abstract" target="_blank" >http://onlinelibrary.wiley.com/doi/10.1002/chir.22534/abstract</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/chir.22534" target="_blank" >10.1002/chir.22534</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    A Solid Phase Vibrational Circular Dichroism Study of Polypeptide-Surfactant Interaction

  • Original language description

    We studied the interaction of poly-l-lysine (PLL) and poly-l-arginine (PLAG) with sodium dodecyl sulfate (SDS) surfactant and the interaction of poly-l-glutamic acid (PLGA) and poly-l-aspartic acid (PLAA) with tetradecyltrimethylammonium bromide (TTAB) surfactant using vibrational circular dichroism (VCD) spectroscopy in the region of C-H stretching vibration and in the Amide I region both in solution and in mulls. A chirality transfer from polypeptides to achiral surfactants was observed in the C-H stretching region, where measurements in solution were impossible. This observation was enabled by a special sample treatment technique using lyophilization and the preparation of mulls. This technique demonstrated itself as an interesting and beneficial tool for VCD measurements. In addition, we observed that SDS changed the secondary structure of PLL to the -sheet and of PLAG to the -helix. TTAB disrupted the PLGA and PLAA structure. These results were obtained in the mull but were confir

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    BO - Biophysics

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GAP208%2F11%2F0105" target="_blank" >GAP208/11/0105: Expanding the Optical Activity Method to the Realm of Biomolecules</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2015

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Chirality

  • ISSN

    0899-0042

  • e-ISSN

  • Volume of the periodical

    27

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    8

  • Pages from-to

    965-972

  • UT code for WoS article

    000364635600014

  • EID of the result in the Scopus database