A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study.
Munier-Lehmann, H
A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study. [electronic resource] - Proteins Aug 1999 - 238-48 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
0887-3585
Adenylate Kinase--chemistry
Amino Acid Sequence
Animals
Circular Dichroism
Cloning, Molecular
Enzyme Stability
Kinetics
Models, Molecular
Molecular Sequence Data
Molecular Weight
Mycobacterium tuberculosis--enzymology
Nuclear Magnetic Resonance, Biomolecular
Protein Denaturation
Protein Structure, Secondary
Recombinant Proteins--biosynthesis
Sequence Alignment
Sequence Homology, Amino Acid
Spectrophotometry, Infrared
Temperature
Tosylphenylalanyl Chloromethyl Ketone
Trypsin--metabolism
A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study. [electronic resource] - Proteins Aug 1999 - 238-48 p. digital
Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
0887-3585
Adenylate Kinase--chemistry
Amino Acid Sequence
Animals
Circular Dichroism
Cloning, Molecular
Enzyme Stability
Kinetics
Models, Molecular
Molecular Sequence Data
Molecular Weight
Mycobacterium tuberculosis--enzymology
Nuclear Magnetic Resonance, Biomolecular
Protein Denaturation
Protein Structure, Secondary
Recombinant Proteins--biosynthesis
Sequence Alignment
Sequence Homology, Amino Acid
Spectrophotometry, Infrared
Temperature
Tosylphenylalanyl Chloromethyl Ketone
Trypsin--metabolism