Structure, stability, and function of hDim1 investigated by NMR, circular dichroism, and mutational analysis

Biochemistry

Volumn 42, Issue 32, 2003, Pages 9609-9618

  Zhang, Yu Zhu ^a,c   Cheng, Hong ^a   Gould, Kathleen L ^b   Golemis, Erica A ^a   Roder, Heinrich ^a  

^a FOX CHASE CANCER CENTER   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c Illinois Institute of Technology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; GENETIC ENGINEERING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

CIRCULAR DICHROISM;

BIOCHEMISTRY;

CYSTEINE; DIM1P PROTEIN; HDIM1 PROTEIN; MESSENGER RNA; MULTIPLE SPLICING ASSOCIATED PROTEIN; PROTEIN; SMALL NUCLEAR RIBONUCLEOPROTEIN; THIOREDOXIN; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; DISULFIDE BOND; MUTATIONAL ANALYSIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; RNA SPLICING; THERMODYNAMICS;

ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; DNA MUTATIONAL ANALYSIS; GUANIDINE; HUMANS; METHYLTRANSFERASES; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OXIDATION-REDUCTION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE DELETION; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 0041525560     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034486i     Document Type: Article

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