Theoretical investigations of oxygen-17 NMR chemical shifts to discriminate among helical forms |
| |
Authors: | De Gortari Itzam Galván Marcelo Ireta Joel Segall Matthew Pickard Chris J Payne Mike |
| |
Institution: | TCM Group, Cavendish Laboratory, University of Cambridge, Madingley Road, Cambridge CB3 0HE, United Kingdom. dego@nmr.mpibpc.mpg.de |
| |
Abstract: | 17O, 15N, 13C, and 1H NMR chemical shieldings are calculated using density functional theory to differentiate among the three primarily helical forms, 310, alpha, and pi in polyalanine peptides under periodic boundary conditions. This study suggests 17O as the best observable, as it has been demonstrated to be sensitive to hydrogen bonding and highly affected by small changes in the polypeptide in helix conformations. This theoretical study seeks to characterize the subtle conformational differences of helical structures by NMR chemical shift observables which may lead to important questions in experimental structure determination on the basis of using chemical shifts to identify protein secondary structures. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|