The V108M mutation decreases the structural stability of catechol O-methyltransferase

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 7-8, 2008, Pages 1098-1105

  Rutherford, K ^a   Alphandery E ^a   McMillan, A ^a   Daggett, V ^a,b   Parson, W W ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b University of Washington   (United States)

Author keywords

Catechol O methyltransferase; Circular dichroism; Fluorescence; Protein stability; Protein structure; Protein unfolding

Indexed keywords

CATECHOL; CATECHOL METHYLTRANSFERASE; GUANIDINE; METHIONINE; S ADENOSYLMETHIONINE; TRYPTOPHAN; VALINE;

ARTICLE; BINDING SITE; CIRCULAR DICHROISM; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE SPECTROSCOPY; GENE MUTATION; LIGHT SCATTERING; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; SINGLE NUCLEOTIDE POLYMORPHISM; TEMPERATURE DEPENDENCE;

CATECHOL O-METHYLTRANSFERASE; CIRCULAR DICHROISM; HUMANS; MODELS, MOLECULAR; MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SCATTERING, RADIATION; SPECTROMETRY, FLUORESCENCE;

EID: 52449135481     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.04.006     Document Type: Article

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