 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](en5571fig3mag.jpg)
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Figure 3
HSQC spectrum of folded, unstructured and apo and ligand-bound proteins. (a) Two-dimensional 1H–15N heteronuclear single-quantum coherence (HSQC) NMR spectrum showing the distinct discrimination in the region below 8.3 p.p.m. in ω1 identifying a folded protein (red, sharp peak contours) compared with the wide and unresolved peaks for disordered protein sample (blue contours). Image courtesy of Simon Colebrook, Department of Biochemistry, Oxford University and Joanne Nettleship, Oxford Protein Production facility. (b) HSQC spectrum of apo and ligand-bound protein. The two-dimensional 1H–15N HSQC NMR spectrum of bacterial methionine aminopeptidase (bMAP) with (right) and without (left) a tightly bound novel inhibitor (Evdokimov et al., 2007  ). Note the drastic improvement in the discrimination of the spectrum for the bMAP–ligand complex compared with the apoprotein. The crystals of the bMAP–ligand complex diffracted to 0.9 Å resolution. Image courtesy of Artem Evdokimov, Procter & Gamble Pharmaceuticals, Mason, Ohio, USA. Figure adapted from Rupp (2015). |
![[Figure 3]](en5571fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
