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Structural Biophysics Laboratory (SBL)
Protein-Nucleic Acid Interaction Section

Research Projects: The 3P Program


individual peptide planes
Proteins are made of individual peptide planes, as shown in the figure below. If the plane orientations, defined by three angles (δ,ρ,γ), are determined, so does a protein backbone structure. The 3P program is based on the intrinsic periodic correlations between residual dipolar couplings (RDCs) and in-plane internuclear vectors, and between RDCs and the orientation of peptide planes relative to an alignment tensor. The program extracts accurate rhombic, axial components of the alignment tensor without explicit coordinates, and discrete peptide plane orientations, which are utilized in combination with readily available phi/psi angles to determine the three-dimensional backbone structures of proteins. The 3P program uses one alignment tensor. We demonstrate the utility and robustness of the program, using both experimental and synthetic data sets, which were added with different levels of noise or were incomplete.

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