NMR and structural data for Connexin 32 and Connexin 26 N-terminal peptides.

ABSTRACT: In this article we present ¹H and ¹³C chemical shift assignments, secondary structural propensity data and normalized temperature coefficient data for N-terminal peptides of Connexin 26 (Cx26), Cx26G12R and Cx32G12R mutants seen in syndromic deafness and Charcot Marie Tooth Disease respectively, published in "Structural Studies of N-Terminal Mutants of Connexin 26 and Connexin 32 Using 1H NMR Spectroscopy" (Y. Batir, T.A. Bargiello, T.L. Dowd, 2016) [1]. The mutation G12R affects the structure of both Cx26 and Cx32 peptides differently. We present data from secondary structure propensity chemical shift analysis which calculates a secondary structure propensity (SSP) score for both disordered or folded peptides and proteins using the difference between the ¹³

SUBMITTER: Batir Y 

PROVIDER: S-EPMC5048080 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature