Engineering thermostability in archaebacterial glyceraldehyde-3-phosphate dehydrogenase Hints for the important role of interdomain contacts in stabilizing protein conformation-Reference-Cited by-同舟云学术

Engineering thermostability in archaebacterial glyceraldehyde-3-phosphate dehydrogenase Hints for the important role of interdomain contacts in stabilizing protein conformation

Published:1990-11-26 Issue:1-2 Volume:275 Page:130-134
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Biro Jutta,Fabry Stefan,Dietmaier Wolfgang,Bogedain Christoph,Hensel Reinhard

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(90)81456-X/fullpdf

Reference12 articles.

1. Purification and characterization of d-glyceraldehyde-3-phosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus

2. Expression of the glyceraldehyde-3-phosphate dehydrogenase gene from the extremely thermophilic archaebacteriumMethanothermus fervidusinE. coli

3. Nucleotide sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from the mesophilic methanogenic archaebacteria Methanobacterium bryantii and Methanobacterium formicicum. Comparison with the respective gene structure of the closely related extreme thermophile Methanothermus fervidus

4. Methanogens: reevaluation of a unique biological group

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