TROSY in NMR studies of the structure and function of large biological macromolecules.
Transverse relaxation-optimized spectroscopy (TROSY), in combination with various isotope-labeling techniques, has opened avenues to study biomolecules with molecular masses of up to 1000000Da by solution NMR. Important recent applications of TROSY include the structure determination of membrane proteins in detergent micelles, structural and functional studies of large proteins in both monomeric form and macromolecular complexes, and investigations of intermolecular interactions in large complexes. TROSY improves the measurement of residual dipolar couplings and the detection of scalar couplings across hydrogen bonds - techniques that promise to further enhance the determination of solution structures of large proteins and oligonucleotides.
Fernández
César
C
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich, CH-8093, Zürich, Switzerland. cesar.fernandez@pharma.novartis.com
Wider
Gerhard
G
D001665:Binding Sites; D001704:Biopolymers / Q000737:chemistry* / Q000378:metabolism; D003461:Crystallography / Q000379:methods*; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008968:Molecular Conformation; D009696:Nucleic Acids / Q000737:chemistry* / Q000378:metabolism; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship
D001704:Biopolymers; D046911:Macromolecular Substances; D008565:Membrane Proteins; D009696:Nucleic Acids; D011506:Proteins