A5036137597- Enzyme Structure and Function
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University of Oulu
2016-2025
Biocenter Finland
2007-2020
University of Jyväskylä
2010-2011
HUN-REN Research Centre for Natural Sciences
2011
Gifu University
2007
University of Antwerp
2002-2006
Purdue University West Lafayette
2005
European Molecular Biology Laboratory
1990-1999
European Molecular Biology Organization
1992-1998
European Molecular Biology Laboratory
1991-1998
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTInteraction of pyrophosphate moieties with .alpha.-helixes in dinucleotide-binding proteinsRik K. Wierenga, Marc C. H. De Maeyer, and Wim G. J. HolCite this: Biochemistry 1985, 24, 6, 1346–1357Publication Date (Print):March 12, 1985Publication History Published online1 May 2002Published inissue 12 March 1985https://pubs.acs.org/doi/10.1021/bi00327a012https://doi.org/10.1021/bi00327a012research-articleACS PublicationsRequest reuse permissionsArticle...
The Src-homology 3 (SH3) region is a protein domain consisting of approximately 60 residues. It occurs in large number eukaryotic proteins involved signal transduction, cell polarization and membrane--cytoskeleton interactions. function unknown, but it probably specific protein--protein Here we report the crystal structure SH3 Fyn (a Src family tyrosine kinase) at 1.9 A resolution. crystals have two molecules per asymmetric unit. These domains are not related by local twofold axis....
The purification and characterization of triose-phosphate isomerase from the psychrophilic bacterium Vibrio marinus (vTIM) is described. Crystal structures vTIM-sulfate complex vTIM-2-phosphoglycolate (at a 2.7-A resolution) are also presented. optimal growth temperature 15 degrees C. Stability studies show that vTIM an unstable protein with half-life only 10 min at 25 sequence most closely related to Escherichia coli TIM (eTIM) (66% identity), several unique structural features described...
The dimeric, peroxisomal 3-ketoacyl-CoA thiolase catalyses the conversion of into acyl-CoA, which is shorter by two carbon atoms. This reaction last step β-oxidation pathway. crystal structure unliganded yeast Saccharomyces cerevisiae has been refined at 1.8 Å resolution. An unusual feature this presence helices, completely buried in dimer and sandwiched between β-sheets. analysis shows that sequences these helices are not hydrophobic, but generate amphipathic helices. helix N-terminal...
Protein engineering on trypanosomal triosephosphate isomerase (TIM) converted this oligomeric enzyme into a stable, monomeric protein that is enzymatically active. Wild-type TIM consists of two identical subunits form very tight dimer involving interactions 32 residues each subunit. By replacing 15 the major interface loop by another 8-residue fragment, variant was constructed stable and with activity. The length, sequence, conformation designed fragment were suggested extensive modeling.