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Science 31 May 1991:
Vol. 252. no. 5010, pp. 1305 - 1308
DOI: 10.1126/science.1925543
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Articles

Science, Vol 252, Issue 5010, 1305-1308
Copyright © 1991 by American Association for the Advancement of Science

articles

Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein

R Nambudripad, W Stark, SJ Opella, and L Makowski

Department of Physics, Boston University, MA 02215.

Filamentous bacteriophage Pf1 assembles by a membrane-mediated process during which the viral DNA is secreted through the membrane while being encapsulated by the major coat protein. Neutron diffraction studies showed that in the virus most of the coat protein consists of two alpha-helical segments arranged end-to-end with an intervening mobile surface loop. Nuclear magnetic resonance studies of the coat protein in the membrane-bound form have shown that the secondary structure is essentially identical to that in the intact virus. A comparison indicates that during membrane-mediated viral assembly, while the secondary structure of the coat protein is largely conserved, its tertiary structure changes substantially.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Pf1 virus structure: helical coat protein and DNA with paraxial phosphates.
D. Liu and L. Day (1994)
Science 265, 671-674
   Abstract »    PDF »
NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
K. Shon, Y Kim, L. Colnago, and S. Opella (1991)
Science 252, 1303-1305
   Abstract »    PDF »


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