Exploring the dihydrodipicolinate synthase tetramer: How resilient is the dimer-dimer interface?

Archives of Biochemistry and Biophysics

Volumn 494, Issue 1, 2010, Pages 58-63

  Griffin, Michael D W ^a   Dobson, Renwick C J ^a   Gerrard, Juliet A ^b   Perugini, Matthew A ^a  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b UNIVERSITY OF CANTERBURY   (New Zealand)

Author keywords

Analytical ultracentrifugation; Dihydrodipicolinate synthase; Oligomer; Protein interface; Protein protein interaction; Quaternary structure

Indexed keywords

DIHYDRODIPICOLINATE SYNTHASE; DIMER; SYNTHETASE; TETRAMER; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME KINETICS; ESCHERICHIA COLI; HYDRODYNAMICS; HYDROGEN BOND; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PHYSICAL CHEMISTRY; POINT MUTATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; STRUCTURE ACTIVITY RELATION; THERMODYNAMICS; ULTRACENTRIFUGATION;

BIOCATALYSIS; BIOPOLYMERS; CIRCULAR DICHROISM; DIMERIZATION; ENZYME STABILITY; HYDRO-LYASES; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; SPECTROPHOTOMETRY, ULTRAVIOLET; ULTRACENTRIFUGATION;

EID: 74149094662     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2009.11.014     Document Type: Article

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