Elimination of the native structure and solubility of the hVAPB MSP domain by the Pro56Ser mutation that causes amyotrophic lateral sclerosis

Biochemistry

Volumn 49, Issue 18, 2010, Pages 3887-3897

  Shi, Jiahai ^a   Lua, Shixiong ^a   Tong, Justina Shihui ^a   Song, Jianxing ^a,b  

^a NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

^b NATIONAL UNIVERSITY OF SINGAPORE   (Singapore)

Author keywords

[No Author keywords available]

Indexed keywords

AMYOTROPHIC LATERAL SCLEROSIS; FREE WATER; HELICAL CONFORMATION; HETERONUCLEAR; INSOLUBLE PROTEINS; NATIVE STRUCTURES; NEUTRAL PH; NMR SPECTROSCOPY; NON-NATIVE; PEPTIDE BONDS; PHYSIOLOGICAL CONDITION; S-SHAPED; SECONDARY STRUCTURES; STRUCTURAL INVESTIGATION; WILD TYPES;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES;

CRYSTAL STRUCTURE;

BUFFER; MAJOR SPERM PROTEIN; MUTANT PROTEIN; PEPTIDE; PROLINE; PROTEIN; PROTEIN NIR2; SERINE; UNCLASSIFIED DRUG; VESICLE ASSOCIATED MEMBRANE PROTEIN ASSOCIATED PROTEIN B;

AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; BETA SHEET; CHEMICAL BOND; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME BINDING; GENE MUTATION; LOSS OF FUNCTION MUTATION; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLUBILITY; STRAIN DIFFERENCE; STRUCTURE ANALYSIS; THERMODYNAMICS; WILD TYPE;

AMINO ACID SEQUENCE; AMYOTROPHIC LATERAL SCLEROSIS; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION, MISSENSE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; SOLUBILITY; THERMODYNAMICS; VESICULAR TRANSPORT PROTEINS;

EID: 77951902249     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi902057a     Document Type: Article

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