The use of proton chemical shifts to define the solution structure of a dimeric peptide.
For flexible peptides, nuclear Overhauser Effects (NOE) experiments do not provide enough information to ensure a correct definition of their solution structure. The use of distance constraints, derived from the knowledge of proton chemical shifts, is developed to restrict the number of possible conformations. In the case of flexible molecules, randomization appears as an important factor of the correct estimation of the chemical shifts from the 3D structure. The refinement of the solution structure of the highly flexible AVP-like parallel dimer is described to illustrate this process.
Busetta
B
B
Laboratoire de Cristallographie, Université Bordeaux I, France.
Picard
P
P
D001127:Arginine Vasopressin / Q000031:analogs & derivatives / Q000138:chemical synthesis / Q000737:chemistry*; D019281:Dimerization; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008962:Models, Theoretical; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D011522:Protons; D011897:Random Allocation; D012996:Solutions
D010455:Peptides; D011522:Protons; D012996:Solutions; D001127:Arginine Vasopressin