Stability, homodimerization, and calcium-binding properties of a single, variant βγ-crystallin domain of the protein absent in melanoma 1 (AIM1)

Biochemistry

Volumn 42, Issue 15, 2003, Pages 4552-4559

  Rajini, Bheemreddy ^a   Graham, Caroline ^b,c   Wistow, Graeme ^b   Sharma, Yogendra ^a  

^a CENTRE FOR CELLULAR AND MOLECULAR BIOLOGY   (India)

^b NATIONAL EYE INSTITUTE   (United States)

^c NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; DIMERIZATION; ESCHERICHIA COLI; MONOMERS; PROTEINS;

HOMODIMERIZATION;

BIOCHEMISTRY;

ABSENT IN MELANOMA 1 PROTEIN; AROMATIC AMINO ACID; BETA CRYSTALLIN; CALCIUM; CALCIUM BINDING PROTEIN; CYSTEINE; GAMMA CRYSTALLIN; LENS PROTEIN; MONOMER; PROTEIN; RECOMBINANT PROTEIN; SPHERULIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; CIRCULAR DICHROISM; COMPARATIVE STUDY; CONCENTRATION RESPONSE; COVALENT BOND; DIMERIZATION; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; GENE OVEREXPRESSION; MOLECULAR CLONING; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; SOLUBILITY; ULTRAVIOLET RADIATION;

AMINO ACID SEQUENCE; CALCIUM; CIRCULAR DICHROISM; CRYSTALLINS; DIMERIZATION; DNA, COMPLEMENTARY; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; SEQUENCE ALIGNMENT; SPECTROMETRY, FLUORESCENCE;

BOVINAE; ESCHERICHIA COLI;

EID: 0344921403     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi027384l     Document Type: Article

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