Identification of proline residues responsible for the slow folding kinetics in pectate lyase C by mutagenesis

Biochemistry

Volumn 41, Issue 14, 2002, Pages 4724-4732

  Kamen, Douglas E ^a,b   Woody, Robert W ^a  

^a Department of Environmental and Radiological Health Sciences   (United States)

^b ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FOLDING KINETICS;

ACTIVATION ENERGY; ISOMERIZATION; MUTAGENESIS; PROTEINS;

BIOCHEMISTRY;

ALANINE; LEUCINE; PECTATE LYASE; PECTATE LYASE C; PROLINE; UNCLASSIFIED DRUG; VALINE;

ARTICLE; CHEMICAL BOND; CIS ISOMER; ENERGY; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; TRANS ISOMER;

BASE SEQUENCE; CALORIMETRY; DNA PRIMERS; ESCHERICHIA COLI; GUANIDINE; ISOENZYMES; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; POLYSACCHARIDE-LYASES; PROLINE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY, ULTRAVIOLET; THERMODYNAMICS; X-RAY DIFFRACTION;

EID: 0037046153     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0115131     Document Type: Article

References (30)