The protein "glass" transition and the role of the solvent

Journal of Physical Chemistry B

Volumn 112, Issue 12, 2008, Pages 3826-3832

  Ngai, K L ^a   Capaccioli, S ^b,c   Shinyashiki, N ^d  

^a NAVAL RESEARCH LABORATORY   (United States)

^b UNIVERSITY OF PISA   (Italy)

^c INFM   (Italy)

^d TOKAI UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; CONFORMATIONS; DYNAMICS; GLASS; GLASS TRANSITION; HYDRATION; HYDROGEN; HYDROGEN BONDS; HYDROPHILICITY; MIXTURES; NONMETALS; PROTEINS; RELAXATION PROCESSES; RELAXATION TIME; SOLVENTS; SUPERCONDUCTING TRANSITION TEMPERATURE; TRUCKS; VAN DER WAALS FORCES;

AMERICAN CHEMICAL SOCIETY (ACS); AQUEOUS MIXTURES; ARRHENIUS; ARRHENIUS ACTIVATION ENERGY; COMPLEX SYSTEMS; DYNAMICAL PROPERTIES; EXPERIMENTAL DATA; GLASS TRANSITION TEMPERATURE (TG); GLASS-FORMERS; GLASS-FORMING; GLASSY STATES; HYDROGEN BONDINGS; HYDROPHILIC GLASS; LOW TEMPERATURE (LTR); PROTEIN MOLECULES; SMALL MOLECULES; SOLVENT RELAXATION; TRANSITION (JEL CLASSIFICATIONS:E52 ,E41 ,E31); TRANSITION TEMPERATURES; VAN DER WAALS;

GLASS BONDING;

GLASS; PROTEIN; SOLVENT; WATER;

ARTICLE; CHEMISTRY; PROTEIN CONFORMATION;

GLASS; PROTEIN CONFORMATION; PROTEINS; SOLVENTS; WATER;

EID: 43049156446     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp710462e     Document Type: Article

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