Version 1
: Received: 20 May 2024 / Approved: 21 May 2024 / Online: 21 May 2024 (09:07:32 CEST)
How to cite:
Alexandrescu, A. T.; Dregni, A. J. The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: Analysis of NMR h3JNC’ Couplings in Four Protein States. Preprints2024, 2024051360. https://doi.org/10.20944/preprints202405.1360.v1
Alexandrescu, A. T.; Dregni, A. J. The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: Analysis of NMR h3JNC’ Couplings in Four Protein States. Preprints 2024, 2024051360. https://doi.org/10.20944/preprints202405.1360.v1
Alexandrescu, A. T.; Dregni, A. J. The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: Analysis of NMR h3JNC’ Couplings in Four Protein States. Preprints2024, 2024051360. https://doi.org/10.20944/preprints202405.1360.v1
APA Style
Alexandrescu, A. T., & Dregni, A. J. (2024). The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: Analysis of NMR <sup>h3</sup>J<sub>NC’</sub> Couplings in Four Protein States. Preprints. https://doi.org/10.20944/preprints202405.1360.v1
Chicago/Turabian Style
Alexandrescu, A. T. and Aurelio J Dregni. 2024 "The Temperature Dependence of Hydrogen Bonds Is More Uniform in Stable Proteins: Analysis of NMR <sup>h3</sup>J<sub>NC’</sub> Couplings in Four Protein States" Preprints. https://doi.org/10.20944/preprints202405.1360.v1
Abstract
Long-range HNCO NMR spectra for proteins show crosspeaks due to 1JNC, 2JNC, 3JNCg and h3JNC couplings. The h3JNC couplings are transmitted through hydrogen bonds and are correlated to hydrogen bond lengths. We collected long-range HNCO data at a series of temperatures for four protein states. 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 isomerization of a single G404-P405 peptide bond. For P22i and CUS-3i the hydrogen bonds detected by NMR agree with those observed in the corresponding domains from cryoEM structures of the two phages. Hydrogen bond lengths derived from the h3JNC couplings, however, are poorly conserved between the distantly related CUS-3i and P22i domains and show differences even between the cis and trans states of HlyIIC. This is consistent with hydrogen bond lengths being determined by local differences in structure rather than the overall folding topology. With increasing temperature hydrogen bonds typically show an apparent increase in length, which has been attributed to protein thermal expansion. Some hydrogen bonds are invariant with temperature, however, while others show apparent decreases in length suggesting they become stabilized with increasing temperature. Considering the data for the three proteins in this study and previously published data for ubiquitin and GB3, lowered protein folding stability and cooperativity correlates with a larger range of temperature responses for hydrogen bonds. This suggests a partial uncoupling of hydrogen bond energetics from global unfolding cooperativity as protein stability decreases.
Keywords
protein folding; m-value; chi-1 angle temperature dependence; structure conservation; NMR structure
Subject
Biology and Life Sciences, Biophysics
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
