Evolutionary Analysis is a Powerful Complement to Energy Calculations Allowing Entropy-Driven Stabilization
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216305%3A26230%2F18%3APU130688" target="_blank" >RIV/00216305:26230/18:PU130688 - isvavai.cz</a>
Result on the web
<a href="https://loschmidt.chemi.muni.cz/peg/wp-content/uploads/2018/09/acscatal18b.pdf" target="_blank" >https://loschmidt.chemi.muni.cz/peg/wp-content/uploads/2018/09/acscatal18b.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acscatal.8b01677" target="_blank" >10.1021/acscatal.8b01677</a>
Alternative languages
Result language
angličtina
Original language name
Evolutionary Analysis is a Powerful Complement to Energy Calculations Allowing Entropy-Driven Stabilization
Original language description
Stability is one of the most important characteristics of proteins employed as biocatalysts, biotherapeutics and biomaterials, and the role of computational approaches in modifying protein stability is rapidly expanding. We have recently identified stabilizing mutations in haloalkane dehalogenase DhaA using phylogenetic analysis, but were not able to reproduce the effects of these mutations using force-field calculations. Here we test four different hypotheses to explain the molecular basis of stabilization using structural, biochemical, biophysical and computational analyses. We demonstrate that protein stabilization by these evolution-based mutations is entropy-driven, in contrast to the enthalpy-driven stabilization by mutations derived from force-field calculations. These results suggest that phylogenetic analysis should always be used to complement energetic calculations in protein stabilization endeavors. Furthermore, the insights gained in this work can stimulate the development of new theoretical approaches for the prediction of entropic contributions to protein stability.
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
10201 - Computer sciences, information science, bioinformathics (hardware development to be 2.2, social aspect to be 5.8)
Result continuities
Project
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Continuities
S - Specificky vyzkum na vysokych skolach
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
ACS Catalysis
ISSN
2155-5435
e-ISSN
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Volume of the periodical
2018
Issue of the periodical within the volume
8
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
9420-9428
UT code for WoS article
000447224100051
EID of the result in the Scopus database
2-s2.0-85053636839