Side Chain Dynamics and Alternative Hydrogen Bonding in the Mechanism of Protein Thermostabilization (Articolo in rivista)

Type
Label
  • Side Chain Dynamics and Alternative Hydrogen Bonding in the Mechanism of Protein Thermostabilization (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Alternative label
  • Khechinashvili* N.N., Fedorov M.V., Kabanov A.V., Monti S., Ghio C., Soda K. (2006)
    Side Chain Dynamics and Alternative Hydrogen Bonding in the Mechanism of Protein Thermostabilization
    in Journal of biomolecular structure & dynamics
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Khechinashvili* N.N., Fedorov M.V., Kabanov A.V., Monti S., Ghio C., Soda K. (literal)
Pagina inizio
  • 255 (literal)
Pagina fine
  • 262 (literal)
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  • 24 (literal)
Rivista
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  • http://www.jbsdonline.com/index.cfm?CFID=13116897&CFTOKEN=73128037&d=3024&c=4216&p=15346&do=detail (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • K.N.N. & K.A.V.: Institute of Cell Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; F.M.V.: Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; M.S. & G.C.: Institute for Physico-Chemical Processes IPCF-CNR, Molecular Modeling Lab, Via G. Moruzzi 1, 56124 Pisa, Italy; S.K.: Department of Bioengineering, Nagaoka University of Technology, Nagaoka 940-2188, Japan (literal)
Titolo
  • Side Chain Dynamics and Alternative Hydrogen Bonding in the Mechanism of Protein Thermostabilization (literal)
Abstract
  • To elucidate the mechanism of protein thermostabilization, the thermodynamic properties of small monomeric proteins from mesophilic and thermophilic organisms have been analyzed. Molecular dynamics simulations were employed in the study of dynamic features of charged and polar side chains of amino acid residues. The basic conclusion has been made: surface charged and polar side chains with high conformational mobility can form alternative hydrogen bonded (H-bonded) donor-acceptor pairs. The correlation between the quantitative content of alternative H-bonds per residue and the temperature of maximal thermostability of proteins has been found. The proposed mechanism of protein thermostabilization suggests continuous disruption of the primary H- bonds and formation of alternative ones, which maintain constant the enthalpy value in the native state and prevent a rapid increase of the conformational entropy with the rising temperature. The analysis of the results show that the more residues located in the N- and C-terminal regions and in the extended loops that are capable of forming alternative longer-range H-bonded pairs, the higher the protein thermostability. (literal)
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