The exclusion of glycine betaine from anionic biopolymer surface: Why glycine betaine is an effective osmoprotectant but also a compatible solute

Biochemistry

Volumn 43, Issue 46, 2004, Pages 14732-14743

  Felitsky, Daniel J ^a,c   Cannon, Jonathan G ^a   Capp, Michael W ^a   Hong, Jiang ^a   Van Wynsberghe, Adam W ^a   Anderson, Charles F ^a   Record Jr , M Thomas ^a,b  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b Scripps Research Institute ^*  (United States)

^c SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOCHEMISTRY; DNA; HYDRATION; STABILITY;

ANIONIC BIOPOLYMER; BINDING DOMAIN; BOVINE SERUM ALBUMIN (BSA);

BIOPOLYMERS;

ALBUMIN; ANION; BETAINE; BIOPOLYMER; CARBOXYLIC ACID DERIVATIVE; DOUBLE STRANDED DNA; HELIX LOOP HELIX PROTEIN; LYSOZYME; PHOSPHATE; POLYANION;

ARTICLE; CIRCULAR DICHROISM; DNA BINDING; ENTHALPY; GLASS TRANSITION TEMPERATURE; GRAVIMETRY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; THERMODYNAMICS; VAPOR PRESSURE;

ANIONS; BACTERIAL PROTEINS; BETAINE; BIOPOLYMERS; CIRCULAR DICHROISM; ENTROPY; ESCHERICHIA COLI PROTEINS; HELIX-TURN-HELIX MOTIFS; MODELS, CHEMICAL; MURAMIDASE; OSMOLAR CONCENTRATION; PROTEIN FOLDING; REPRESSOR PROTEINS; SERUM ALBUMIN, BOVINE; SOLUTIONS; SURFACE PROPERTIES; TEMPERATURE;

BOVINAE;

EID: 8744225646     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049115w     Document Type: Article

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