Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 25 Angstroms Resolution. [electronic resource]
Producer: 19960605Description: 2597-609 p. digitalISSN:- 0006-2960
- Amino Acid Sequence
- Binding Sites
- Crystallography, X-Ray
- Electrochemistry
- Enzyme Stability
- Glyceraldehyde-3-Phosphate Dehydrogenases -- chemistry
- Hydrogen Bonding
- Models, Molecular
- Molecular Sequence Data
- Molecular Structure
- Protein Conformation
- Sequence Homology, Amino Acid
- Thermodynamics
- Thermus -- enzymology
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.
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