Determining a helical protein structure using peptide pixels.
The residual dipolar coupling-periodicity planarity correlation makes it possible to determine peptide plane orientations in regular periodic protein secondary structure elements. Each peptide plane orientation represents a "pixel" of protein structure, and is expressed in terms of three angles referred to as tilt, phase, and pitch angles. In this report, we present the novel "3P" (periodicity, planarity, and pixels) method that allows one to determine secondary and tertiary structure of alpha-helical proteins. We demonstrate the 3P method by determining the structure of domain 1 of the receptor-associated protein (RAP) to a backbone accuracy of 1.0 Angstrom using RDCs measured in a single alignment medium, together with a minimal number of NOE distance restraints, using a new Xplor-NIH module.
Walsh
Joseph D
JD
Protein Nucleic Acid Interaction Section, Structural Biophysics Laboratory, NCI-Frederick, NIH, Frederick, MD 21702, USA.
Kuszweski
John
J
Wang
Yun-Xing
YX
D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*
D011506:Proteins