The role of water in protein's behavior: The two dynamical crossovers studied by NMR and FTIR techniques

Computational and Structural Biotechnology Journal

Volumn 13, Issue , 2015, Pages 33-37

  Mallamace, Francesco ^a,b   Corsaro, Carmelo ^a   Mallamace, Domenico ^a   Vasi, Sebastiano ^a   Vasi, Cirino ^b   Dugo, Giacomo ^a  

^a UNIVERSITY OF MESSINA   (Italy)

^b CNR   (Italy)

Author keywords

Amide bending mode; HR MAS; Hydration water; Lysozyme unfolding; Protein dynamic transition

Indexed keywords

AMIDE; CARBONYL DERIVATIVE; LYSOZYME; WATER;

ARTICLE; ENZYME ACTIVITY; ENZYME DENATURATION; EVOLUTION; HIGH TEMPERATURE; HYDRATION; HYDROGEN BOND; HYDROPHILICITY; INFRARED SPECTROSCOPY; LOW TEMPERATURE; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; WATER ANALYSIS; WATER TEMPERATURE;

EID: 84934290770     PISSN: None     EISSN: 20010370     Source Type: Journal    
DOI: 10.1016/j.csbj.2014.11.007     Document Type: Article

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