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The Use of Proton Chemical Shifts to Define the Solution Structure of a Dimeric Peptide

✍ Scribed by Bernard Busetta; Philippe Picard


Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
559 KB
Volume
2
Category
Article
ISSN
1075-2617

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✦ Synopsis


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.


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