{'fraction_non_alphanumeric': 0.0283436669619132, 'fraction_numerical': 0.01948627103631532, 'mean_word_length': 5.420454545454546, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Solid‐state NMR Structure Determination

Biological applications of solid‐state NMR (SS‐NMR) have been predominantly in the area of model membrane systems. Increasingly the focus has been membrane peptides and proteins. SS‐NMR is able to provide information about how the peptides or proteins interact with the lipids or other peptides/proteins in the membrane, their effect on the membrane and the location of the peptides or proteins relative to the membrane surface. Recent developments in biological SS‐NMR have been made possible by improvements in labelling and NMR techniques. This review discusses aligned systems and magic angle spinning techniques, bilayers and bicelles, and measurement of chemical shift anisotropy and dipolar coupling. A number of specific experiments such as cross polarization, rotational resonance, REDOR, PISEMA, MAOSS and multidimensional experiments are described. In addition to 2H, 13C and 15N, recent solid‐sate 1H, 19F and 17O NMR work is discussed. Several examples of the use of SS‐NMR to determine the structure of membrane peptides and proteins are given. IUBMB Life, 55: 515‐523, 2003