Factors Stabilizing beta-Sheets in Protein Structures from a Quantum-Chemical Perspective
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F19%3A00508834" target="_blank" >RIV/61388963:_____/19:00508834 - isvavai.cz</a>
Result on the web
<a href="https://pubs.acs.org/doi/10.1021/acs.jpcb.9b04866" target="_blank" >https://pubs.acs.org/doi/10.1021/acs.jpcb.9b04866</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.jpcb.9b04866" target="_blank" >10.1021/acs.jpcb.9b04866</a>
Alternative languages
Result language
angličtina
Original language name
Factors Stabilizing beta-Sheets in Protein Structures from a Quantum-Chemical Perspective
Original language description
Protein folds are determined by the interplay between various (de)stabilizing forces, which can be broadly divided into a local strain of the protein chain and intramolecular interactions. In contrast to the alpha-helix, the beta-sheet secondary protein structure is significantly stabilized by long-range interactions between the individual beta-strands. It has been observed that quite diverse amino acid sequences can form a very similar small beta-sheet fold, such as in the three-beta-strand WW domain. Employing 'calibrated' quantum-chemical methods, we show herein on two sequentially diverse examples of the WW domain that the internal strain energy is higher in the beta-strands and lower in the loops, while the interaction energy has an opposite trend. Low strain energy computed for peptide sequences in the loop 1 correlates with its postulated early formation in the folding process. The relatively high strain energy within the beta-strands (up to 8 kcal mol(-1) per amino acid residue) is compensated by even higher intramolecular interaction energy (up to 15 kcal mol(-1) per residue). It is shown in a quantitative way that the most conserved residues across the structural family of WW domains have the highest contributions to the intramolecular interaction energy. On the other hand, the residues in the regions with the lowest strain are not conserved. We conclude that the internal interaction energy is the physical quantity tuned by evolution to define the beta-sheet protein fold.
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
10403 - Physical chemistry
Result continuities
Project
<a href="/en/project/GA17-24155S" target="_blank" >GA17-24155S: Exploring Conformational Space of Short Peptides by Advanced Quantum Chemical and Solvation Methods: A Key to Understand Protein Structures?</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2019
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
123
Issue of the periodical within the volume
30
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
6453-6461
UT code for WoS article
000479326100008
EID of the result in the Scopus database
2-s2.0-85070551693