Related ArticlesFormation of periodic ?-turns in ?/?-hybrid peptides: DFT and NMR experimental evidence.
Chem Asian J. 2014 Feb;9(2):457-61
Authors: Chandrasekhar S, Rao KV, Seenaiah M, Naresh P, Devi AS, Jagadeesh B
Abstract
Hybrid peptidic oligomers comprising natural and unnatural amino acid residues that can exhibit biomolecular folding and hydrogen-bonding mimicry have attracted considerable interest in recent years. While a variety of hybrid peptidic helices have been reported in the literature, other secondary structural patterns such as ?-turns and ribbons have not been well explored so far. The present work reports the design of novel periodic ?-turns in the oligomers of 1:1 natural-?/unnatural trans-?-norborenene (TNAA) amino acid residues. Through DFT, NMR, and MD studies, it is convincingly shown that, in the mixed conformational pool, the heterogeneous backbone of the hybrid peptides preferentially adopt periodic 8-membered (pseudo ?-turn)/7-membered (inverse ?-turn) hydrogen bonds in both polar and non-polar solvent media. It is observed that the stereochemistry and local conformational preference of the ?-amino acid building blocks have a profound influence on accessing the specific secondary fold. These findings may be of significant relevance for the development of molecular scaffolds that facilitate desired positioning of functional side-chains.
Type I and II β-turns prediction using NMR chemical shifts
Type I and II β-turns prediction using NMR chemical shifts
Abstract
A method for predicting type I and II β-turns using nuclear magnetic resonance (NMR) chemical shifts is proposed. Isolated β-turn chemical-shift data were collected from 1,798 protein chains. One-dimensional statistical analyses on chemical-shift data of three classes β-turn (type I, II, and VIII) showed different distributions at four positions, (i) to (iÂ*+Â*3). Considering the central two residues of type I β-turns, the mean values of Cο, Cα, HN, and NH chemical shifts...
nmrlearner
Journal club
0
06-19-2014 10:21 PM
[NMR paper] Type I and II ?-turns prediction using NMR chemical shifts.
Type I and II ?-turns prediction using NMR chemical shifts.
Related Articles Type I and II ?-turns prediction using NMR chemical shifts.
J Biomol NMR. 2014 May 17;
Authors: Wang CC, Lai WC, Chuang WJ
Abstract
[NMR paper] Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 inte
Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 interaction revealed from histidine line broadening.
Related Articles Proton NMR study of peptides from myelin basic protein: evidence for Lys74-His77 interaction revealed from histidine line broadening.
Biochim Biophys Acta. 1996 Mar 7;1293(1):23-30
Authors: Koshy KM, Hashim GA, Boggs JM
Residues 69-84 of guinea pig myelin basic protein contain the encephalitogenic determinant for the Lewis rat. Insertion of histidine and glycine at positions 77 and 78 in bovine...
Formation of periodic ?-turns in ?/?-hybrid peptides: DFT and NMR experimental evidence.
Linear Mode
