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Time-Resolved Protein Side-Chain Motions Unraveled by High-Resolution Relaxometry and Molecular Dynamics Simulations

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F18%3A00104556" target="_blank" >RIV/00216224:14740/18:00104556 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1021/jacs.8b09107" target="_blank" >http://dx.doi.org/10.1021/jacs.8b09107</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/jacs.8b09107" target="_blank" >10.1021/jacs.8b09107</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Time-Resolved Protein Side-Chain Motions Unraveled by High-Resolution Relaxometry and Molecular Dynamics Simulations

  • Original language description

    Motions of proteins are essential for the performance of their functions. Aliphatic protein side chains and their motions play critical roles in protein interactions: for recognition and binding of partner molecules at the surface or serving as an entropy reservoir within the hydrophobic core. Here, we present a new NMR method based on high-resolution relaxometry and high-field relaxation to determine quantitatively both motional amplitudes and time scales of methyl-bearing side chains in the picosecond-to-nanosecond range. We detect a wide variety of motions in isoleucine side chains in the protein ubiquitin. We unambiguously identify slow motions in the low nanosecond range, which, in conjunction with molecular dynamics computer simulations, could be assigned to transitions between rotamers. Our approach provides unmatched detailed insight into the motions of aliphatic side chains in proteins and provides a better understanding of the nature and functional role of protein side-chain motions.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10402 - Inorganic and nuclear chemistry

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

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

    Journal of the American Chemical Society

  • ISSN

    0002-7863

  • e-ISSN

  • Volume of the periodical

    140

  • Issue of the periodical within the volume

    41

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    10

  • Pages from-to

    13456-13465

  • UT code for WoS article

    000447953600045

  • EID of the result in the Scopus database

    2-s2.0-85054139114