In vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site

Proceedings of the National Academy of Sciences of the United States of America

Volumn 105, Issue 49, 2008, Pages 19258-19263

  Sedlák, Erik ^a   Ziegler, Lynn ^c   Kosman, Daniel J ^c   Wittung Stafshede, Pernilla ^a,b  

^a RICE UNIVERSITY   (United States)

^b UMEÅ UNIVERSITY   (Sweden)

^c UNIVERSITY AT BUFFALO   (United States)

Author keywords

Calorimetry; Copper binding protein; Cupredoxin; Spectroscopy

Indexed keywords

APOPROTEIN; CERULOPLASMIN; GLYCAN; PROTEIN FET3P; UNCLASSIFIED DRUG;

ARTICLE; CALORIMETRY; IN VITRO STUDY; PH MEASUREMENT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE; SPECTROSCOPY;

AZURIN; BINDING SITES; CALORIMETRY; CERULOPLASMIN; COPPER; ENDOPLASMIC RETICULUM; GLYCOSYLATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SPECTRUM ANALYSIS;

SACCHAROMYCES CEREVISIAE;

EID: 58049221115     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0806431105     Document Type: Article

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