01383naa a2200217 a 450000100080000000500110000800800410001910000190006024501220007926000090020130000170021052005630022765300170079065300070080765300300081465300190084470000150086370000210087870000180089977302480091710265902010-03-02       1986    bl ---       0--  u    #d1 aCOLNAGO, L. A.  aDirect comparison of the membrane bound and structural forms of the coat protein of the filamentous bacteriophage fd.  c1986  ap. 147 - 158  aThe coat protein of the filamentous bacteriophage fd exists in a membrane bound form as well as in the structural form of the virus during its lifecycle. The changes in the dynamics of the coat protein that accompany the infection of E. coli and the assembly new virus particles are described with NMR experiments. Solid state NMR is used to describe the dynamics of isotopically labelled peptide backbone and amino acid sidechain sites. Motional averaging of powder pattern lineshapes gives qualitative information about the amplitudes and rates of motions.  aCoat protein  aFd  aFilamentous bacteriophage  aMembrane bound1 aLEO, G. C.1 aVALENTINE, K. G.1 aOPELLA, S. J.  tIn: SARMA, R.H.; SARMA, M.H., ed. Biomolecular stereodynamics III: proceedings of the Fourth Conversation in the Discipline Biomolecular Stereodynamics, State University of New York, Albany, NY, June 04-09, 1985. New York: Adenine Press, 1986.