Tracking interactions that stabilize the dimer structure of starch phosphorylase from Corynebacterium callunae. Roles of Arg234 and Arg242 revealed by sequence analysis and site-directed mutagenesis.

Griessler, Richard

Tracking interactions that stabilize the dimer structure of starch phosphorylase from Corynebacterium callunae. Roles of Arg234 and Arg242 revealed by sequence analysis and site-directed mutagenesis. [electronic resource] - European journal of biochemistry May 2003 - 2126-36 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

0014-2956

10.1046/j.1432-1033.2003.03562.x doi


Allosteric Site
Amino Acid Sequence
Arginine--chemistry
Binding Sites
Blotting, Southern
Circular Dichroism
Cloning, Molecular
Corynebacterium--enzymology
DNA--metabolism
Dimerization
Escherichia coli--metabolism
Gene Library
Glucans--metabolism
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data
Mutagenesis, Site-Directed
Oligonucleotides--pharmacology
Plasmids--metabolism
Protein Structure, Quaternary
Protein Structure, Tertiary
Recombinant Proteins--chemistry
Sequence Homology, Amino Acid
Starch Phosphorylase--chemistry
Temperature