De novo design of a non-local beta-sheet protein with high stability and accuracy
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F18%3A00104596" target="_blank" >RIV/00216224:14740/18:00104596 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1038/s41594-018-0141-6" target="_blank" >http://dx.doi.org/10.1038/s41594-018-0141-6</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41594-018-0141-6" target="_blank" >10.1038/s41594-018-0141-6</a>
Alternative languages
Result language
angličtina
Original language name
De novo design of a non-local beta-sheet protein with high stability and accuracy
Original language description
beta-sheet proteins carry out critical functions in biology, and hence are attractive scaffolds for computational protein design. Despite this potential, de novo design of all-beta-sheet proteins from first principles lags far behind the design of all-alpha or mixed-alpha beta domains owing to their non-local nature and the tendency of exposed beta-strand edges to aggregate. Through study of loops connecting unpaired beta-strands (beta-arches), we have identified a series of structural relationships between loop geometry, side chain directionality and beta-strand length that arise from hydrogen bonding and packing constraints on regular beta-sheet structures. We use these rules to de novo design jellyroll structures with double-stranded beta-helices formed by eight antiparallel beta-strands. The nuclear magnetic resonance structure of a hyperthermostable design closely matched the computational model, demonstrating accurate control over the beta-sheet structure and loop geometry. Our results open the door to the design of a broad range of non-local beta-sheet protein structures.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/LQ1601" target="_blank" >LQ1601: CEITEC 2020</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
NATURE STRUCTURAL & MOLECULAR BIOLOGY
ISSN
1545-9993
e-ISSN
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Volume of the periodical
25
Issue of the periodical within the volume
11
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
1028
UT code for WoS article
000449271800009
EID of the result in the Scopus database
2-s2.0-85055985092