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Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Protein folding is slaved to solvent motions
H Frauenfelder1, P W Fenimore, G Chen
1Theory Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA. frauenfelder@lanl.gov
Summary
Protein folding rates are controlled by solvent alpha-fluctuations, a process termed slaving. This model explains folding speed by linking it to solvent dynamics and protein conformational substates.
Area of Science:
- Biophysics
- Protein Dynamics
- Chemical Kinetics
Background:
- Proteins fold from amino acid chains into functional structures.
- Folding times vary significantly, from microseconds to hours.
- The precise control mechanisms governing protein folding rates remain debated.
Purpose of the Study:
- To propose a model for protein folding rates based on solvent dynamics.
- To investigate the role of alpha-fluctuations in protein folding.
- To explain the observed slowness of protein folding compared to solvent fluctuations.
Main Methods:
- Postulating a 'slaving' model where protein motions are dictated by solvent fluctuations.
- Applying the slaving concept to both folded protein motions and the folding process itself.
- Analyzing the temperature dependence and rate coefficients of folding and solvent fluctuations.
Main Results:
- Protein folding exhibits the same temperature dependence as solvent alpha-fluctuations but proceeds much slower.
- The slaving model suggests folding rate is governed by solvent dynamics (k(alpha)) and the number of protein conformational substates.
- Activation enthalpy of folding is primarily influenced by the solvent.
Conclusions:
- Protein folding is a 'slaved' process, where conformational changes are controlled by solvent dynamics.
- The folding rate (k(f)) is significantly slower than solvent fluctuations (k(alpha)) due to the vast number of accessible unfolded protein substates.
- Beta-fluctuations may influence late stages of protein folding.
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