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The effect of protein composition on hydration dynamics
O Rahaman1, S Melchionna, D Laage
1Laboratoire de Biochimie Théorique, CNRS, UPR9080, Université Paris Diderot, Sorbonne Paris Cité, Institut de Biologie Physico-Chimique, Paris, France.
Physical Chemistry Chemical Physics : PCCP
|February 6, 2013
Summary
Protein surface water dynamics are similar regardless of amino acid sequence or temperature when folded. Unfolding proteins alters water dynamics, slowing them down significantly due to topological effects on hydrogen bonds.
Area of Science:
- Biophysics
- Protein dynamics
- Water-protein interactions
Background:
- Understanding protein surface water dynamics is crucial for comprehending protein function and stability.
- Homologous proteins with varying thermal resistances offer a unique system to study the influence of sequence and structure on hydration.
Purpose of the Study:
- To investigate how protein structure and amino acid composition affect water dynamics at the protein-surfaces.
- To determine the impact of temperature on surface water dynamics in both folded and unfolded states.
Main Methods:
- Utilizing advanced spectroscopic techniques to probe water dynamics at protein interfaces.
- Comparing water dynamics across two homologous proteins with distinct thermal properties.
- Analyzing temperature-dependent changes in water mobility.
Main Results:
- Surface water dynamics of folded homologous proteins are insensitive to amino acid composition and exhibit similar temperature responses.
- Upon protein unfolding, surface water dynamics slow down by a factor of two compared to bulk water.
- The observed changes are attributed to the protein's topological influence on water hydrogen bond networks.
Conclusions:
- Protein topology, rather than specific amino acid composition, primarily dictates surface water dynamics.
- Protein unfolding significantly alters the interfacial water structure and dynamics.
- These findings provide insights into the fundamental principles governing protein hydration and stability.
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