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
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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
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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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
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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
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