๐”– Bobbio Scriptorium
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Frictional coefficients of multisubunit structures. II. Application to proteins and viruses

โœ Scribed by V. Bloomfield; K. E. Van Holde; W. O. Dalton


Publisher
Wiley (John Wiley & Sons)
Year
1967
Tongue
English
Weight
650 KB
Volume
5
Category
Article
ISSN
0006-3525

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โœฆ Synopsis


The theory of Kirkwood for the translational frictional coefficients of structures composed of identical subunits has been extended in the previous paper t.o the case where nonidentical snbiinits are involved. In this paper, the t.heory is applied to particular proteins and viruses. It is found that t,he calculated sedimentation coefficients of various states of aggregation of the reversibly associating proteins hemocyanin and phycocyanin are in excellent agreement with experiment. The dimensions of the fibrinogen moleciile obtained from electron micrographs do not give good agreement bet,weeri calculated and experimental frictional coefficients. The frictional coefficient of tobacco mosaic virus calculated without explicit consideration of end effects is in good agreement with experiment if a hydrodynamic diameter of 180 A., corresponding to the maximum diameter from x-ray studies, is used. Agreement is also good for the faqt, sedimenting form of bacteriophage T2 and the protein ghosts of bacteriophage A ; but, the slow form of T2 and whole A have frictional coefficients considerably in excess of those calculated. Tail fiber confignration or head porosity are unable to account for the difference in sedimentat~ion coefficients between the fast and slow forms of T2.

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