The goal of structure determination based on experimental NMR data is to find molecular structures that satisfy the experimental data, such as measured resonance intensities, and have a low energy in terms of a molecular potential energy function. The technique of restraining only the average molecular properties with respect to the measured values is investigated and further developed.
The application of MD techniques in crystallographic refinement is further developed and tested. As in the NMR case, the application of time-averaged structure factor restraints leads to a better representation of the measurement. The full anharmonic and anisotropic motions of the atoms are taken into account. The problem of obtaining reasonably good initial phases to be used in structure refinement of proteins is tackled using a general low resolution representation of such molecules.
Major Algorithmic Contributions
- Use of MD for protein structure refinement based on NMR data [85.01]
- Use of time-averaged distance restraints in protein structure determination based on NMR data [89.04]
- Use of time-averaged restraints in protein structure determination based on X-ray data [93.18, 95.02, 99.15]
- A method for biomolecular structure refinement based on adaptive restraints using local-elevation simulation [07.29, 09.17]
- An improved conformational clustering algorithm [10.04]
- A method for biomolecular structure refinement based on NMR order parameters [14.12]