Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F10%3A00342433" target="_blank" >RIV/61388963:_____/10:00342433 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues
Original language description
Here, we present the design and analysis of highly active (200?500%) insulin analogues that are truncated at residue 26 of the B-chain (B26). They show a structural convergence in the form of a new (beta)-turn at B24-B26. We propose that the key elementin insulin?s transition, from an inactive to an active state, may be the formation of the (beta)-turn at B24-B26 associated with a trans to cis isomerisation at the B25-B26 peptide bond.
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
CC - Organic chemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proceedings of the National Academy of Sciences of the United States of America
ISSN
0027-8424
e-ISSN
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Volume of the periodical
107
Issue of the periodical within the volume
5
Country of publishing house
US - UNITED STATES
Number of pages
5
Pages from-to
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UT code for WoS article
000274296300031
EID of the result in the Scopus database
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