The coat proteins of filamentous phage are first synthesized as transmem-brane proteins and then assembled onto the extruding viral particles. We
investigated the transmembrane conformation of the Pseudomonas aerugi-nosa Pf3 phage coat protein using proton-decoupled
solid-state NMR spectroscopy.
The format of this Chapter will be slightly different from that for earlier years.
Papers dealing with essentially static situations will be dealt with first – with
each Group of the Periodic Table discussed in turn. Results on dynamic
systems will then follow – again on the basis of the Periodic Groups, with
papers on paramagnetic compounds being dealt with last.
Cellulose and wheat straw degradation byRuminococcus albuswas moni-tored using NMR spectroscopy. In situ solid-state
magic angle spinning NMR was used to monitor the modification of the
composition and structure of cellulose and
C-enriched wheat straw during
the growth of the bacterium on these substrates.
Proteins are occasionally converted from their normal soluble state to
highly ordered fibrillar aggregates (amyloids), which give rise to pathologi-cal conditions that range from neurodegenerative disorders to systemic
amyloidoses. Recent methodological advances in solid-state NMR and
EPR spectroscopy have enabled determination of the 3D structure of sev-eral amyloids at residue-level resolution.
The membrane binding affinity of the pleckstrin homology (PH) domain of
phospholipase C (PLC)-d1 was investigated using a vesicle coprecipitation
assay and the structure of the membrane-associated PH domain was
probed using solid-state
C NMR spectroscopy.