Cavities of α1-antitrypsin that play structural and functional roles

Protein Science

Volumn 10, Issue 7, 2001, Pages 1446-1453

  Lee, Cheolju ^a,c   Maeng, Jin Soo ^a,d   Kocher, Jean Pierre ^b,e   Lee, Byungkook ^b   Yu, Myeong Hee ^a  

^a Korea Institute of Science and Technology   (South Korea)

^b NATIONAL CANCER INSTITUTE   (United States)

^c NORTHWESTERN UNIVERSITY   (United States)

^d NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

^e Camitro Corporation   (United States)

Author keywords

1 antitrypsin; Cavity filling mutations; Conformational stability; Molecular packing; Native strain

Indexed keywords

ALPHA 1 ANTITRYPSIN; CARBENE; SERINE PROTEINASE INHIBITOR;

ARTICLE; CONFORMATIONAL TRANSITION; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

ALPHA 1-ANTITRYPSIN; AMINO ACID SUBSTITUTION; ANIMALS; DRUG STABILITY; GUANIDINE; MUTAGENESIS, SITE-DIRECTED; PANCREATIC ELASTASE; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; SWINE;

EID: 0034976979     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.840101     Document Type: Article

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