Stereoselective deuterium labeling of proR beta-protons in the NMR structure determination of a helix-turn-helix turn peptide mimic.
The NMR structure of a small, side-chain-cyclized tripeptide mimic of the turn in the helix-turn-helix (HTH) motif was determined. The four beta-protons were stereospecifically assigned by stereoselective deuterium replacement of only the proR beta-protons. All 24 of 30 NOESY cross-peaks not involving chemically defined or freely rotating protons, and six of seven coupling constants from the P.COSY were used as distance and angle constraints in molecular modeling. MacroModel found 33/1000 structures in the NMR constrained search and 263/1000 structures in the unconstrained search, indicating meaningful constraint by the NMR data. However, the 10 lowest-energy structures from the unconstrained and constrained searches are very similar, so modeling alone was able to find the experimentally determined structure.
Etzkorn
F A
FA
Department of Chemistry, University of Virginia, Charlottesville 22904-4319, USA. etzkorn@virginia.edu
Travins
J M
JM
D003903:Deuterium / Q000737:chemistry*; D019077:Helix-Turn-Helix Motifs; D008958:Models, Molecular; D008968:Molecular Conformation; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D010456:Peptides, Cyclic / Q000737:chemistry*; D011487:Protein Conformation; D011522:Protons
D010456:Peptides, Cyclic; D011522:Protons; D003903:Deuterium