Proteins in organic solvents

Mattos, Carla; Ringe, Dagmar

doi:10.1016/s0959-440x(01)00278-0

Cited by 165 publications

(148 citation statements)

References 41 publications

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“…Proteins in hydrophobic solvent are thought to retain their native structure as a result of kinetic trapping due to stronger intramolecular hydrogen bonding and a more rigid structure in the absence of water (46). The structure of small peptides like mersacidin can, however, vary remarkably in different envi- .…”

Section: Substantial Chemical Shift Changes Indicate a Strong Dependementioning

confidence: 99%

NMR Study of Mersacidin and Lipid II Interaction in Dodecylphosphocholine Micelles

Hsu

Breukink

Bierbaum

et al. 2003

Journal of Biological Chemistry

125

119

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Section: Substantial Chemical Shift Changes Indicate a Strong Dependementioning

confidence: 99%

NMR Study of Mersacidin and Lipid II Interaction in Dodecylphosphocholine Micelles

Hsu

Breukink

Bierbaum

et al. 2003

Journal of Biological Chemistry

125

119

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“…In recent years a number of cosolvents have found a wide range of uses in biology: as cryosolvents, protein denaturants, protein fold stabilizers, protein function modulators, and more. 30 In the present work methanol was used as cryosolvent. Methanol preserves protein structure and function at moderate concentrations although at higher concentration it tends to denature protein structure and promotes helix formation.…”

Section: Introductionmentioning

confidence: 99%

Temperature and timescale dependence of protein dynamics in methanol : water mixtures

Tournier

Réat

Dunn

et al. 2005

Phys. Chem. Chem. Phys.

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Experimental and computer simulation studies have suggested the presence of a transition in the dynamics of hydrated proteins at around 180-220 K. This transition is manifested by nonlinear behaviour in the temperature dependence of the average atomic mean-square displacement which increases at high temperature. Here, we present results of a dynamic neutron scattering analysis of the transition for a simple enzyme: xylanase in water : methanol solutions of varying methanol concentrations. In order to investigate motions on different timescales, two different instruments were used: one sensitive to B100 ps timescale motions and the other to Bns timescale motions. The results reveal distinctly different behaviour on the two timescales examined. On the shorter timescale the dynamics are dictated by the properties of the surrounding solvent: the temperature of the dynamical transition lowers with increasing methanol concentration closely following the melting behaviour of the corresponding water : methanol solution. This contrasts with the longer (ns) timescale results in which the dynamical transition appears at temperatures lower than the corresponding melting point of the cryosolvent. These results are suggested to arise from a collaborative effect between the protein surface and the solvent which lowers the effective melting temperature of the protein hydration layer. Taken together, the results suggest that the protein solvation shell may play a major role in the temperature dependence of protein solution dynamics.

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“…As a result, the drive to unfold is large in hydrophobic organic solvents, but the protein lacks the conformational flexibility necessary to unfold. On the other hand, in more polar organic solvents such as dimethylformamide or dimethylsulfoxide, the protein tends to unfold due to the combined effects of somewhat increased protein flexibility and favorable interactions between solvent and hydrophobic amino acid side chains in the absence of the hydrophobic effect induced by water [14,15].…”

Section: General Properties Of Water and Its Interaction With Proteinsmentioning

confidence: 99%

“…It defines the three dimensional structure of a protein primarily due to two factors. First, water plays a fundamental role in favoring the weak van der Waals attractions between hydrophobic residues at the core through the hydrophobic effect [15][16][17]. This is a result of the nonpolar groups on the protein surface promoting the interactions among the water molecules themselves [18].…”

Section: General Properties Of Water and Its Interaction With Proteinsmentioning

confidence: 99%

Minimizing frustration by folding in an aqueous environment

Mattos

Clark

2008

Archives of Biochemistry and Biophysics

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Although life as we know it evolved in an aqueous medium, the properties of water are not completely understood. In this review, we focus on the role of water in guiding protein folding and stability. Specifically, we discuss the mechanisms of protein folding in an aqueous environment, the effects of water on the folding energy landscape as well as the transition state ensemble, and interactions of water with the folded state. We show that water cannot be viewed as a passive solvent, but rather, plays a very active role in the life of a protein.

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Proteins in organic solvents

Cited by 165 publications

References 41 publications

NMR Study of Mersacidin and Lipid II Interaction in Dodecylphosphocholine Micelles

NMR Study of Mersacidin and Lipid II Interaction in Dodecylphosphocholine Micelles

Temperature and timescale dependence of protein dynamics in methanol : water mixtures

Minimizing frustration by folding in an aqueous environment

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