Allosteric Effect of Adenosine Triphosphate on Peptide Recognition by 3 ' 5 '-Cyclic Adenosine Monophosphate Dependent Protein Kinase Catalytic Subunits
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F16%3A00093864" target="_blank" >RIV/00216224:14740/16:00093864 - isvavai.cz</a>
Result on the web
<a href="http://link.springer.com/article/10.1007%2Fs10930-016-9691-9" target="_blank" >http://link.springer.com/article/10.1007%2Fs10930-016-9691-9</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s10930-016-9691-9" target="_blank" >10.1007/s10930-016-9691-9</a>
Alternative languages
Result language
angličtina
Original language name
Allosteric Effect of Adenosine Triphosphate on Peptide Recognition by 3 ' 5 '-Cyclic Adenosine Monophosphate Dependent Protein Kinase Catalytic Subunits
Original language description
The allosteric influence of adenosine triphosphate (ATP) on the binding effectiveness of a series of peptide inhibitors with the catalytic subunit of 3'5'-cyclic adenosine monophosphate dependent protein kinase was investigated, and the dependence of this effect on peptide structure was analyzed. The allosteric effect was calculated as ratio of peptide binding effectiveness with the enzyme-ATP complex and with the free enzyme, quantified by the competitive inhibition of the enzyme in the presence of ATP excess, and by the enzyme-peptide complex denaturation assay, respectively It was found that the principle "better binding-stronger allostery" holds for interactions of the studied peptides with the enzyme, indicating that allostery and peptide binding with the free enzyme are governed by the same specificity pattern.
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
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
The Protein Journal
ISSN
1572-3887
e-ISSN
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Volume of the periodical
35
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
8
Pages from-to
459-466
UT code for WoS article
000389918500008
EID of the result in the Scopus database
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