Related Experiment Video
Updated: Nov 4, 2025
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Structural Stability and Conformational Dynamics of Cytochrome c in Hydrated Deep Eutectic Solvents
Sk Saddam Hossain1, Sneha Paul1, Anunay Samanta1
1School of Chemistry, University of Hyderabad, Hyderabad 500046, India.
Deep eutectic solvents (DESs) impact protein structure. Trimethylglycine-based DESs with ethylene glycol (EG) fully unfold cytochrome c, while those with glycerol (GL) only slightly alter it, revealing solvent interaction importance.
Area of Science:
- Biophysical Chemistry
- Protein Dynamics
- Green Solvents
Background:
- Deep eutectic solvents (DESs) are emerging as eco-friendly alternatives in biological applications.
- Understanding solvent effects on biomolecule structure is vital for their successful use.
- Cytochrome c (Cytc) is a key protein for studying biomolecular interactions in novel media.
Purpose of the Study:
- To investigate the influence of two trimethylglycine (TMG)-based DESs (with ethylene glycol [EG] and glycerol [GL]) on the structural stability and dynamics of Cytc.
- To compare the effects of TMG-EG and TMG-GL on Cytc structure and dynamics.
Main Methods:
- Single-molecule fluorescence correlation spectroscopy (FCS) to measure Cytc size and conformational dynamics.
- Ensemble-based biophysical techniques to assess protein structure.
- Utilized A488-labeled and wild-type Cytc for comprehensive analysis.
Main Results:
- FCS revealed Cytc size (20.5 ± 1.5 Å) and dynamics (54 ± 2 μs) in buffer, which were altered by DESs.
- TMG-EG significantly influenced Cytc size and dynamics, leading to complete unfolding.
- TMG-GL caused only slight alterations in Cytc structure, indicating differential solvent effects.
Conclusions:
- The structural behavior of Cytc in hydrated DESs depends on the interaction strength between DES components and water.
- TMG-EG is a potent denaturant for Cytc, while TMG-GL exhibits milder effects.
- These findings are crucial for designing and utilizing DESs in biorelated applications.
More Related Videos
08:54Vibrational Spectra of a N719-Chromophore/Titania Interface from Empirical-Potential Molecular-Dynamics Simulation, Solvated by a Room Temperature Ionic Liquid
Published on: January 25, 2020
09:49Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
Related Concept Videos
01:09Complexation Equilibria: Factors Influencing Stability of Complexes
02:30Stability of Substituted Cyclohexanes
The two chair conformations of cyclohexanes undergo rapid interconversion at room temperature. Both forms have identical energies and stabilities, each comprising equal amounts of the equilibrium mixture. Replacing a hydrogen atom with a functional group makes the two conformations energetically non-equivalent.
For example, in...
01:22Protein Folding
00:52¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
01:17Chemical Shift: Internal References and Solvent Effects
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
01:28Stability of Conjugated Dienes
A comparison of the enthalpies of hydrogenation of dienes reveals that conjugated dienes release less heat on hydrogenation, rendering them more stable than their nonconjugated analogs.