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Propagating conformational changes over long (and short) distances in proteins
1Department of Molecular and Cell Biology, University of California, Berkeley 94720-3206, USA.
Summary
Protein conformational changes are driven by ligand binding between evolved states. Binding energy and transition speed are optimized for physiological function, supported by aspartate receptor data.
Area of Science:
- Biochemistry and Molecular Biology
- Structural Biology
- Biophysics
Background:
- Proteins undergo conformational changes to perform functions.
- Understanding how these changes propagate is crucial for protein function.
- Ligand binding often triggers conformational shifts.
Purpose of the Study:
- To model the propagation of long-distance conformational changes in proteins.
- To investigate the evolutionary selection of protein states and transition kinetics.
- To support the model using crystallographic data of an aspartate receptor.
Main Methods:
- Modeling ligand-induced conformational changes between two protein states.
- Analyzing evolutionary selection of pathway kinetics.
- Utilizing crystallographic data of wild-type and mutant aspartate receptors.
Main Results:
- Conformational change propagation fits a model of ligand-induced transitions between evolved states.
- Kinetics are selected for physiologically appropriate ligand binding energy and transition speed.
- Crystallographic data of aspartate receptor variants support the proposed model.
Conclusions:
- Protein conformational changes are governed by ligand-induced transitions between evolutionarily selected states.
- The kinetics of these transitions are fine-tuned for optimal physiological function.
- The aspartate receptor serves as a validated example of this mechanism.
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