Hydration of guanidinium depends on its local environment.

Molecular dynamics studies on the denaturation of polyalanine in the presence of guanidinium chloride at low concentration

Molecular dynamic simulation is a powerful method that monitors all variations in the atomic level in explicit solvent. By this method we can calculate many chemical and biochemical properties of large scale biological systems. In this work all-atom molecular dynamics simulation of polyalanine (PA) was investigated in the presence of 0.224, 0.448, 0.673, 0.897 and 1.122 M of guanidinium chlorid...

Hydration of guanidinium depends on its local environment† †Electronic supplementary information (ESI) available: Full citation for ref. 51, experimental details and reproducibility of the IRPD measurements, comparison between experimental IRPD spectra with harmonic IR spectra of energetic low lying isomers for [Gdm(H2O)n]+, n = 6–9, structures of the energetic low lying isomers of [Gdm(H2O)n]+, n = 6–9, and representative structures of [Gdm(H2O)n]+, [Na(H2O)n]+, [TMA(H2O)n]+, with n = 20 and 40. Quantitative comparison of the spectra for Gdm+, Na+ and TMA+ with n = 20–100 in the HB stretching region. See DOI: 10.1039/c5sc00618j Click here for additional data file.

Effect of the Protein Denaturants Urea and Guanidinium on Water Structure: A Structural and Thermodynamic Study

The mechanism of the denaturing effects of urea and the guanidinium ion on proteins is still an unsolved and important problem in protein chemistry. Changes in the hydrogen bond network of water in the first hydration shell of urea and guanidinium were analyzed in terms of the random network model using Monte Carlo simulations. Bulk water consists of two populations of hydrogen bonds: a predomi...

Collective hydration dynamics of guanidinium chloride solutions and its possible role in protein denaturation: a terahertz spectroscopic study.

The remarkable ability of guanidinium chloride (GdmCl) to denature proteins is a well studied yet controversial phenomenon; the exact molecular mechanism is still debatable, especially the role of hydration dynamics, which has been paid less attention. In the present contribution, we have addressed the issue of whether the collective hydrogen bond dynamics of water gets perturbed in the presenc...

Protein Denaturants at Aqueous–Hydrophobic Interfaces: Self-Consistent Correlation between Induced Interfacial Fluctuations and Denaturant Stability at the Interface

The notion of direct interaction between denaturing cosolvent and protein residues has been proposed in dialogue relevant to molecular mechanisms of protein denaturation. Here we consider the correlation between free energetic stability and induced fluctuations of an aqueous-hydrophobic interface between a model hydrophobically associating protein, HFBII, and two common protein denaturants, gua...