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Reversal of the Hofmeister Series: Specific Ion Effects on Peptides

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F13%3A00395118" target="_blank" >RIV/61388963:_____/13:00395118 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1021/jp405683s" target="_blank" >http://dx.doi.org/10.1021/jp405683s</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/jp405683s" target="_blank" >10.1021/jp405683s</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Reversal of the Hofmeister Series: Specific Ion Effects on Peptides

  • Original language description

    Ion-specific effects On salting-in and salting-out of proteins, protein denaturation, as well as enzymatic activity are typically rationalized in terms of the Hofmeister Here, we demonstrate by means of NMR spectroscopy and, molecular dynamics simulations that the traditional explanation of the Hofmeister ordering of ions in term of their bulk hydration properties is inadequate. Using triglycine as a model system, we show that the Hofmeister series for anions changes from a direct to a reversed series upon uncapping the N- terminus. Weakly hydrated anions, such as iodide and thio cyanate, interact with the peptide bond; while strongly hydrated anions like sulfate are repelled from it. In Contrast reversed order in interactions, of anions is observed atthe positively charged, uncapped N-terminus, and by analogy, this should also be the case at side chains of positively,Charged amino These results demonstrate that the specific chemical and physical properties, of peptides and proteins p

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    CF - Physical chemistry and theoretical chemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GBP208%2F12%2FG016" target="_blank" >GBP208/12/G016: Controlling structure and function of biomolecules at the molecular scale: theory meets experiment</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2013

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Journal of Physical Chemistry B

  • ISSN

    1520-6106

  • e-ISSN

  • Volume of the periodical

    117

  • Issue of the periodical within the volume

    27

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    9

  • Pages from-to

    8150-8158

  • UT code for WoS article

    000321884100011

  • EID of the result in the Scopus database