ArticleBiophysical journal2012
Effects of Hofmeister ions on the α-helical structure of proteins.
Article in Biophysical journal, 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, 58 citations in OpenAlex.
- Assessment of methods for evaluating structural stability of cell envelope fragments in hypersaline brines as biosignatures of ancient microbial life.Scientific reports · 2025Article
- Article
- Hofmeister Effect in RT-QuIC Seeding Activity of Chronic Wasting Disease Prions.Frontiers in bioengineering and biotechnology · 2021Article
- FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin and Trypsin under Neutral Salts.Biomolecules · 2020Article
- Computing on actin bundles network.Scientific reports · 2019Article
- Tyrosine Rotamer States in Beta Amyloid: Signatures of Aggregation and Fibrillation.ACS omega · 2018Article
- Divalent magnesium cation concentrations determine the formation of tofu-like precipitates with differing urea solubilities.Heliyon · 2018Article
- 'Reverse' Hofmeister effects on the sol-gel transition rates for an α-helical peptide-PEG bioconjugate.Physical chemistry chemical physics : PCCP · 2018Article
- The Thermodynamics of Anion Complexation to Nonpolar Pockets.The journal of physical chemistry. B · 2018Article
- Ion-induced alterations of the local hydration environment elucidate Hofmeister effect in a simple classical model of Trp-cage miniprotein.Journal of molecular modeling · 2017Article
- Covalent dye attachment influences the dynamics and conformational properties of flexible peptides.PloS one · 2017Article
- Scorpion toxins prefer salt solutions.Journal of molecular modeling · 2015Article
- Hydration of guanidinium depends on its local environment.Chemical science · 2015Article
- Conformational free-energy landscapes for a peptide in saline environments.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molecular conformation of proteins is sensitive to the nature of the aqueous environment. In particular, the presence of ions can stabilize or destabilize (denature) protein secondary structure. The underlying mechanisms of these actions are still not fully understood. Here, we combine circular dichroism (CD), single-molecule Förster resonance energy transfer, and atomistic computer simulations to elucidate salt-specific effects on the structure of three peptides with large α-helical propensity. CD indicates a complex ion-specific destabilization of the α-helix that can be rationalized by using a single salt-free computer simulation in combination with the recently introduced scheme of ion-partitioning between nonpolar and polar peptide surfaces. Simulations including salt provide a molecular underpinning of this partitioning concept. Furthermore, our single-molecule Förster resonance energy transfer measurements reveal highly compressed peptide conformations in molar concentrations of NaClO(4) in contrast to strong swelling in the presence of GdmCl. The compacted states observed in the presence of NaClO(4) originate from a tight ion-backbone network that leads to a highly heterogeneous secondary structure distribution and an overall lower α-helical content that would be estimated from CD. Thus, NaClO(4) denatures by inducing a molten globule-like structure that seems completely off-pathway between a fully folded helix and a coil state.
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