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Modeling conformational change in macromolecules as an elastic deformation.
1Crystallography Laboratory, NCI-Frederick Cancer Research and Development Center, Maryland 21701.
Proteins
|January 1, 1991
Summary
Macromolecules like proteins and nucleic acids exhibit elasticity. Analyzing structural deviations beyond rigid superposition reveals valuable information about their dynamic conformational changes.
Area of Science:
- Structural Biology
- Biophysics
- Computational Chemistry
Background:
- Macromolecules, including nucleic acids and proteins, exist in multiple conformations.
- Current methods often compare structures using rigid body superposition, neglecting molecular flexibility.
Purpose of the Study:
- To investigate the information contained within the deviations from rigid body superposition in macromolecular structures.
- To treat these deviations as elastic deformations of a common molecular structure.
Main Methods:
- Analysis of atomic structures of macromolecules in different conformations.
- Application of elastic deformation models to structural comparison.
- Case studies on deoxyhemoglobin vs. carbonmonoxyhemoglobin and catabolite gene activator protein conformations.
Main Results:
- Deviations from rigid superposition contain significant information about molecular dynamics.
- Treating these deviations as elastic deformations allows for the extraction of this information.
- Demonstrated utility in comparing hemoglobin variants and protein conformational states.
Conclusions:
- Elastic deformation analysis offers a more comprehensive approach to comparing macromolecular structures.
- This method enhances understanding of protein and nucleic acid conformational flexibility.
- Provides insights into the functional implications of structural variations.