Thermal coefficients of the methyl groups within ubiquitin

Physiological processes such as protein folding and molecular recognition are intricately linked to their dynamic signature, which is reflected in their thermal coefficient. In addition, the local conformational entropy is directly related to the degrees of freedom, which each residue possesses with...

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Veröffentlicht in:	Protein science 2012-04, Vol.21 (4), p.562-570
Hauptverfasser:	Sabo, T. Michael, Bakhtiari, Davood, Walter, Korvin F. A., McFeeters, Robert L., Giller, Karin, Becker, Stefan, Griesinger, Christian, Lee, Donghan
Format:	Artikel
Sprache:	eng
Schlagworte:	Carbon Isotopes - chemistry cross‐correlated relaxation Entropy Group dynamics Humans methyl group dynamics Methylation Molecular Dynamics Simulation NMR Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Folding Protein Stability Temperature thermal coefficients Time Factors ubiquitin Ubiquitin - chemistry
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