The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: An Analysis of NMR ^h3J_NC' Couplings in Four Different Protein Structures.

ABSTRACT: Long-range HNCO NMR spectra for proteins show crosspeaks due to ¹J_NC', ²J_NC', ³J_NCγ, and ^h3J_NC' couplings. The ^h3J_NC' couplings are transmitted through hydrogen bonds and their sizes are correlated to hydrogen bond lengths. We collected long-range HNCO data at a series of temperatures for four protein structures. P22i and CUS-3i are six-stranded beta-barrel I-domains from phages P22 and CUS-3 that share less than 40% sequence identity. The cis and trans states of the C-terminal domain from pore-forming toxin hemolysin ΙΙ (HlyIIC) arise from the isomerization of a single G404-P405 peptide bond. For P22i and CUS-3i, hydrogen bonds detected by NMR agree with those observ

SUBMITTER: Alexandrescu AT 

PROVIDER: S-EPMC11243222 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature