The ultrahigh resolution crystal structure of ribonuclease A containing an isoaspartyl residue: Hydration and sterochemical analysis

Journal of Molecular Biology

Volumn 297, Issue 3, 2000, Pages 713-732

  Esposito, Luciana ^a   Vitagliano, Luigi ^a   Sica, Filomena ^a   Sorrentino, Giosuè ^a   Zagari, Adriana ^a   Mazzarella, Lelio ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

Crystal structure; Deamidation; RNase A; Structure function relationship; Ultrahigh resolution

Indexed keywords

ASPARTIC ACID DERIVATIVE; HYDROGEN; ISOASPARTIC ACID; PANCREATIC RIBONUCLEASE; RIBONUCLEASE A; SOLVENT; SULFATE; UNCLASSIFIED DRUG; WATER;

ACCURACY; ARTICLE; CRYSTAL STRUCTURE; DEAMINATION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; HYDRATION; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; REACTION ANALYSIS; STEREOCHEMISTRY; STRUCTURE ANALYSIS;

BOVINAE;

EID: 0034737316     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3597     Document Type: Article

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