Recent Developments in Biomolecular Solid-State NMR - Recent Developments in Biomolecular NMR - page 318

CHAPTER 13
Recent Developments in
Biomolecular Solid-State NMR
VICTORIA A. HIGMAN AND ANTHONY WATTS*
Biomembrane Structure Unit, Biochemistry Department, South Parks Road,
University of Oxford, Oxford, OX1 3QU, UK
*E-mail: [e-mail]
13.1 Introduction
Over the past decade biomolecular solid-state NMR has undergone a period of
rapid development and expansion. Solid-state NMR has the advantage that
samples need neither be soluble nor exhibit long-range order as they do for
solution NMR or X-ray crystallography, respectively. Thus high-resolution
structural studies of numerous systems (e.g., amyloid fibrils, membrane
proteins in their native lipid environment, cytoskeleton binding proteins)
which are not possible by other methods, are becoming accessible and have
driven interest in the technique.
Since the determination of the first full protein structure using solid-state
magic angle spinning (MAS) NMR in 2002 1 structural studies of a wide variety
of samples have been reported and developments of pulse sequences, hardware
technology, sample preparation techniques and isotopic labelling have
continued to push the boundaries of the method. Spectral resolution and
crowding of resonances, and sensitivity, remain the chief challenges.
Alongside solid-state MAS NMR, static solid-state NMR using oriented
samples has long been a useful tool for studying membrane proteins, in
particular small helical peptides. 2,3 More recently, structure-function relation-
ships have been resolved, notably the function of membrane-embedded ion