Zobrazeno 1 - 10
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pro vyhledávání: '"K U, Yüksel"'
Publikováno v:
The Journal of biological chemistry. 269(7)
Covalent modification of Glu165 in the catalytic center of triose-phosphate isomerase with the substrate analogue 3-chloroacetol phosphate traps the complex in two conformations. The two resulting 31P NMR resonances at 6.9 and 5.7 ppm appear to refle
Publikováno v:
The Journal of biological chemistry. 268(36)
Limited proteolysis of the triose-phosphate isomerase (EC 5.3.1.1) by subtilisin generates peptides that remain noncovalently attached and catalytically active. Edman degradation of the peptides showed that the primary proteolytic sites for yeast tri
Publikováno v:
The Journal of biological chemistry. 267(28)
The effects of unfolding, refolding, and hybridization of triosephosphate isomerase (TPI) subunits from different species and subunits which have been specifically modified at the active site have been examined. These effects have been evaluated in t
Publikováno v:
Progress in clinical and biological research. 344
Publikováno v:
Basic life sciences. 35
Publikováno v:
Journal of chromatography. 265(1)
Autor:
Korshunov, D. A., Kondakova, I. V.
Publikováno v:
AIP Conference Proceedings; 2016, Vol. 1760 Issue 1, p1-6, 6p, 2 Black and White Photographs, 2 Graphs
Publikováno v:
Soft Matter; 11/21/2009, Issue 22, p4549-4555, 7p
Autor:
Michael R. Lynch
The fields of molecular evolution, genome evolution, and evolutionary genetics are now well-established. Remarkably, however, although all evolutionary modifications begin at the cellular level, and despite the advances made in cell biology and micro
Autor:
Daniel L. Purich, R. Donald Allison
Biochemical kinetics refers to the rate at which a reaction takes place. Kinetic mechanisms have played a major role in defining the metabolic pathways, the mechanistic action of enzymes, and even the processing of genetic material. The Handbook of B