[34] Structural basis of thermostability in hyperthermophilic proteins, or “There's more than one way to skin a cat”
- 1 January 2001
- book chapter
- Published by Elsevier
- Vol. 334, 469-478
- https://doi.org/10.1016/s0076-6879(01)34486-5
Abstract
No abstract availableThis publication has 32 references indexed in Scilit:
- Hyperthermostable Protein Structure Maintained by Intra and Inter-helix Ion-pairs in Archaeal O6-Methylguanine-DNA MethyltransferaseJournal of Molecular Biology, 1999
- Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricusJournal of Molecular Biology, 1999
- Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interfaceJournal of Molecular Biology, 1999
- Crystal structure of the thermostable archaeal intron-encoded endonuclease I- Dmo I 1 1Edited by I. A. WilsonJournal of Molecular Biology, 1999
- Refined crystal structure of a superoxide dismutase from the hyperthermophilic archaeon Sulfolobus acidocaldarius at 2.2 Å resolutionJournal of Molecular Biology, 1999
- Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosusJournal of Molecular Biology, 1998
- The structure of a trimeric archaeal adenylate kinaseJournal of Molecular Biology, 1998
- Ferredoxin from the hyperthermophile Thermotoga maritima is stable beyond the boiling point of waterJournal of Molecular Biology, 1997
- Crystal Structure at 2.0 Å Resolution of Phosphoribosyl Anthranilate Isomerase from the Hyperthermophile Thermotoga maritima: Possible Determinants of Protein Stability,Biochemistry, 1997
- Determinants of Enzyme Thermostability Observed in the Molecular Structure ofThermusaquaticusd-Glyceraldehyde-3-phosphate Dehydrogenase at 2.5 Å Resolution,Biochemistry, 1996