Biological Magnetic Resonance, Volume 16Lawrence J. Berliner, Jacques Reuben Plenum Press, 1978 - Biology |
Contents
Determining Structures of Large Proteins and Protein | 3 |
Chapter | 5 |
Additional Methods of Structure Refinement | 15 |
Copyright | |
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¹³C aliphatic amino acids applied assignment backbone angle bilayers Biochemistry Biol Biomol calculated calmodulin carbon Chem chemical shift Clore coherence constant-time correlation coupling constants cross-correlated cross-correlated relaxation cross-peak D₂O decoupling deuterium dihedral angle dipolar coupling distance restraints E.COSY experimental Figure frequency fully protonated G₁ Gardner Griesinger Gronenborn Grzesiek heteronuclear HNCA homonuclear HSQC Hu and Bax interaction isotopic isotopomers Karplus Kupče LeMaster linewidths Magn measured membrane proteins methods methyl groups Metzler micelles molecules multiplet NMR spectroscopy NOESY NOESY experiments nuclei obtained Opella peak peptide perdeuterated protein phase PLCC Protein NMR protons pulse sequence relaxation rates residues resolution Reson sample secondary structure sensitivity SH2 domain shown in Fig sidechain solid-state NMR solution NMR spectra spectrum spin systems structure determination t₁ t₂ tensor TOCSY torsion angle triple-resonance uniformly 15N labeled values Vuister Wang and Bax Yamazaki