Some measurements of the shape and hydrodynamic properties of yeast phosphoglycerate kinase (E.C.2.7.2.3)

Using values obtained for sedimentation and diffusion constants the relative mass of phosphoglycerate kinase was calculated to be 45 800 ± 1700. This value is higher than was previously estimated and the difference is thought to be caused by contamination of earlier crystalline preparations- Using t...

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Bibliographic Details
Published in:Biophysical chemistry 1979-03, Vol.9 (3), p.215-221
Main Authors: Smith, Janet, Spragg, S.P.
Format: Article
Language:English
Subjects:
Molecular Weight
Phosphoglycerate Kinase
Protein Conformation
Saccharomyces cerevisiae - enzymology
X-Ray Diffraction
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Summary:Using values obtained for sedimentation and diffusion constants the relative mass of phosphoglycerate kinase was calculated to be 45 800 ± 1700. This value is higher than was previously estimated and the difference is thought to be caused by contamination of earlier crystalline preparations- Using the coordinates from X-ray crystallography it was found possible to calculate a frictional ratio for a linear dumb-bell (1.115) which compared well with the ratio calculated from diffusion (1.114 ± 0.033). Since the calculated ratio for a bent molecule was 1.020 the natural state of the molecule in solution is essentially linear. From the concentration dependence of sedimentation and diffusion was calculated the effective interactive radius which resembles haemoglobin in its relationship to the molecular radius.
ISSN:0301-4622
1873-4200
DOI:10.1016/0301-4622(79)85004-8