Deamidation of Human γs-Crystallin Increases Attractive Protein Interactions: Implications for Cataract

Biochemistry

Volumn 54, Issue 31, 2015, Pages 4890-4899

  Pande, Ajay ^a   Mokhor, Natalya ^a,b   Pande, Jayanti ^a  

^a STATE UNIVERSITY OF NEW YORK   (United States)

^b SALUS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CHEMICAL REACTIONS; ELECTROPHORESIS; LIGHT SCATTERING; OPACITY; PHASE SEPARATION; PROTEINS; SPECTROSCOPIC ANALYSIS;

GUANIDINIUM HYDROCHLORIDE; LIQUID-LIQUID PHASE SEPARATION; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN-PROTEIN INTERACTIONS; REPULSIVE INTERACTIONS; SECOND VIRIAL COEFFICIENTS; SECONDARY AND TERTIARY STRUCTURES; STATIC LIGHT SCATTERING;

RECOMBINANT PROTEINS;

ASPARAGINE; GAMMA CRYSTALLIN; GLUTAMINE; CRYGS PROTEIN, HUMAN;

AMINO ACID SEQUENCE; ARTICLE; CATARACT; CONTROLLED STUDY; DEAMINATION; ESCHERICHIA COLI; HUMAN; HYDROGEN BOND; IN VITRO STUDY; ISOELECTRIC FOCUSING; LIGHT SCATTERING; NONHUMAN; PHASE SEPARATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; CHEMICAL MODEL; CHEMISTRY; METABOLISM;

ASPARAGINE; CATARACT; GAMMA-CRYSTALLINS; GLUTAMINE; HUMANS; MODELS, CHEMICAL; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84938696796     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00185     Document Type: Article

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