Two-, three-, and four-dimensional nuclear magnetic resonance spectroscopy of protein pharmaceuticals.
Advances in NMR spectroscopy and related computational methods continue at a rapid pace. In the past three years, the capability to make complete assignments of protein spectra has expanded from a limit of approximately 100 residues to a limit of possibly 400 residues via isotope-edited three- and four-dimensional methods.
Vander Velde
D G
DG
NMR Laboratory, University of Kansas, Lawrence 66045, USA.
Matsuura
J
J
Manning
M C
MC
D000818:Animals; D001709:Biotechnology; D004815:Epidermal Growth Factor / Q000737:chemistry; D006801:Humans; D007328:Insulin / Q000737:chemistry; D007378:Interleukins / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D015394:Molecular Structure; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013678:Technology, Pharmaceutical; D013816:Thermodynamics
D007328:Insulin; D007378:Interleukins; D011506:Proteins; D004815:Epidermal Growth Factor