ArticleBiochemistry2012
Temperature dependence of water interactions with the amide carbonyls of α-helices.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
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- Plant-Based Protein Bioinks with Transglutaminase Crosslinking: 3D Printability and Molecular Insights from NMR and Synchrotron-FTIR.Foods (Basel, Switzerland) · 2026Article
- Transition Dipole Strength as a Quantitative Tool for Protein Secondary Structure Analysis.The journal of physical chemistry. B · 2025Article
- Chasing weakly-bound biological water in aqueous environment near the peptide backbone by ultrafast 2D infrared spectroscopy.Communications chemistry · 2024Article
- High Throughput Proteomic Exploration of Hypothermic Preservation Reveals Active Processes within the Cell Associated with Cold Ischemia Kinetic.International journal of molecular sciences · 2021Article
- Comparative modelling studies of fruit bromelain using molecular dynamics simulation.Journal of molecular modeling · 2020Article
- Influence of Membrane-Fusogen Distance on the Secondary Structure of Fusogenic Coiled Coil Peptides.Langmuir : the ACS journal of surfaces and colloids · 2019Article
- Article
- Heterogeneity in the Folding of Villin Headpiece Subdomain HP36.The journal of physical chemistry. B · 2018Article
- Submillisecond Dynamics of Mastoparan X Insertion into Lipid Membranes.The journal of physical chemistry letters · 2016Article
- Anisotropic energy flow and allosteric ligand binding in albumin.Nature communications · 2014Article
- Deducing conformational variability of intrinsically disordered proteins from infrared spectroscopy with Bayesian statistics.Chemical physics · 2013Article
- Early turn formation and chain collapse drive fast folding of the major cold shock protein CspA of Escherichia coli.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Hydration is a key determinant of the folding, dynamics, and function of proteins. In this study, temperature-dependent Fourier transform infrared (FTIR) spectroscopy combined with singular value decomposition (SVD) and global fitting were used to investigate both the interaction of water with α-helical proteins and the cooperative thermal unfolding of these proteins. This methodology has been applied to an isolated α-helix (Fs peptide) and to globular α-helical proteins including the helical subdomain and full-length villin headpiece (HP36 and HP67). The results suggest a unique IR signature for the interaction of water with the helical amide carbonyl groups of the peptide backbone. The IR spectra indicate a weakening of the net hydrogen bond strength of water to the backbone carbonyls with increasing temperature. This weakening of the backbone solvation occurs as a discrete transition near the maximum of the temperature-dependent hydrophobic effect, not a continuous change with increasing temperature. Possible molecular origins of this effect are discussed with respect to previous molecular dynamics simulations of the temperature-dependent solvation of the helix backbone.
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