Literature DB >> 372185

Small angle X-ray scattering of dimeric yeast hexokinase in solution.

R C McDonald, D M Engelman, T A Steitz.   

Abstract

Small angle x-ray scattering measurements on dimeric yeast hexokinase B at pH 5.5 in acetate buffer yield a radius of gyration of 31.28 +/- 0.23 angstrom. This measured value is comparable to the radius of gyration of 31.5 angstrom calculated from the refined coordinates of the dimer in the BII crystal form. The hexokinase dimer found in the BI crystal form has a radius of gyration of 42 angstrom calculated from the atomic coordinates. Thus, the measured radius of gyration is consistent with the BII dimer being the predominant species in solution and rules out the existence of the BI dimer as a major species under these conditions.

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Year:  1979        PMID: 372185

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  2 in total

1.  Crystal structure of hexokinase KlHxk1 of Kluyveromyces lactis: a molecular basis for understanding the control of yeast hexokinase functions via covalent modification and oligomerization.

Authors:  E Bartholomeus Kuettner; Karina Kettner; Antje Keim; Dmitri I Svergun; Daniela Volke; David Singer; Ralf Hoffmann; Eva-Christina Müller; Albrecht Otto; Thomas M Kriegel; Norbert Sträter
Journal:  J Biol Chem       Date:  2010-10-12       Impact factor: 5.157

2.  Electrospray ionization mass spectrometry of biotin binding to streptavidin.

Authors:  K Eckart; J Spiess
Journal:  J Am Soc Mass Spectrom       Date:  1995-10       Impact factor: 3.109

  2 in total

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