title: Improved methods for structural studies of proteins using nuclear magnetic resonance spectroscopy.
abstract: The past few years have seen the development of three- and four-dimensional heteronuclear nuclear magnetic resonance methods. Increased sophistication in labelling strategies, use of pulse-field gradients and the application of these methods at higher magnetic fields has, in combination with improved software, allowed studies of the structure, interactions and dynamics of significantly larger proteins (now up to approximately 270 amino acid residues).
authors.affiliation: Department of Biochemistry, University of Cambridge, UK.
authors.forename: R T
authors.initials: RT
authors.lastname: Clowes
authors.forename: A
authors.initials: A
authors.lastname: Crawford
authors.forename: A R
authors.initials: AR
authors.lastname: Raine
authors.forename: B O
authors.initials: BO
authors.lastname: Smith
authors.forename: E D
authors.initials: ED
authors.lastname: Laue
mesh_terms: D000818:Animals; D004798:Enzymes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D012680:Sensitivity and Specificity
chemical_list: D004798:Enzymes; D011506:Proteins