ArticleBiochemistry2009
Salt dependence of an alpha-helical peptide folding energy landscapes.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 34 citations in OpenAlex.
- Sequence-encoded differences in the conformational ensembles of CITED transcriptional activation domains impact coactivator binding.Protein science : a publication of the Protein Society · 2026Article
- Sequence-encoded differences in the conformational ensembles of CITED transcriptional activation domains impact coactivator binding.bioRxiv : the preprint server for biology · 2026Article
- The lac repressor hinge helix in context: The effect of the DNA binding domain and symmetry.Biochimica et biophysica acta. General subjects · 2020Article
- Why Proteins are Big: Length Scale Effects on Equilibria and Kinetics.The protein journal · 2019Review
- Glutamine and Asparagine Side Chain Hyperconjugation-Induced Structurally Sensitive Vibrations.The journal of physical chemistry. B · 2015Article
- Association of polyalanine and polyglutamine coiled coils mediates expansion disease-related protein aggregation and dysfunction.Human molecular genetics · 2014Article
- Prediction of protein relative enthalpic stability from molecular dynamics simulations of the folded and unfolded states.Biophysical journal · 2012Article
- Impact of ion binding on poly-L-lysine (un)folding energy landscape and kinetics.The journal of physical chemistry. B · 2012Article
- Conformation of poly-L-glutamate is independent of ionic strength.Biophysical chemistry · 2012Article
- Direct observations of conformational distributions of intrinsically disordered p53 peptides using UV Raman and explicit solvent simulations.The journal of physical chemistry. A · 2011Article
- UV resonance Raman finds peptide bond-Arg side chain electronic interactions.The journal of physical chemistry. B · 2011Article
- Circular dichroism and UV resonance raman study of the impact of alcohols on the Gibbs free energy landscape of an alpha-helical peptide.Biochemistry · 2010Article
- Sodium perchlorate effects on the helical stability of a mainly alanine peptide.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
We used CD, UV resonance Raman spectroscopy, and molecular dynamics simulation to examine the impact of salts on the conformational equilibria and the Ramachandran Psi angle (un)folding Gibbs free energy landscape coordinate of a mainly polyalanine alpha-helical peptide, AP of sequence AAAAA(AAARA)(3)A. NaClO(4) stabilizes alpha-helical-like conformations more than does NaCl, which stabilizes more than Na(2)SO(4) at identical ionic strengths. This alpha-helix stabilization ordering is the reverse of the Hofmeister series of anions in their ability to disorder water hydrogen bonding. Much of the NaClO(4) alpha-helix stabilization results from ClO(4)(-) association with the AP terminal -NH(3)(+) groups and Arg side chains. ClO(4)(-) stabilizes 3(10)-helix conformations but destabilizes turn conformations. The decreased Cl(-) and SO(4)(2-) AP alpha-helix stabilization probably results from a decreased association with the Arg and terminal -NH(3)(+) groups. Cl(-) is expected to have a smaller binding affinity and thus stabilizes alpha-helical conformations intermediately between NaClO(4) and Na(2)SO(4). Electrostatic screening stabilizes pi-bulge conformations.
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Registered trials
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