title: Geometry of kinked protein helices from NMR data.
abstract: Mathematical questions related to determining the structure of a protein from NMR orientational restraints are discussed. The protein segment is a kinked alpha helix modeled as a regular alpha helix in which two adjacent torsion angles have been varied from their ideal values. Varying these torsion angles breaks the helix into two regular helical segments joined at a kink. The problem is to find the torsion angles at the kink from the relationship of the helical segments to the direction of the magnetic field.
authors.affiliation: Institute of Molecular Biophysics, Florida State University, Kasha Laboratory, Tallahassee, FL 32306, USA. dmurray@magnet.fsu.edu
authors.forename: Dylan T
authors.initials: DT
authors.lastname: Murray
authors.forename: Yuanting
authors.initials: Y
authors.lastname: Lu
authors.forename: T A
authors.initials: TA
authors.lastname: Cross
authors.forename: J R
authors.initials: JR
authors.lastname: Quine
mesh_terms: D000465:Algorithms; D016880:Anisotropy; D019295:Computational Biology / Q000379:methods*; D008433:Mathematics; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000295:instrumentation / Q000379:methods*; D011487:Protein Conformation
chemical_list: D008565:Membrane Proteins; D009587:Nitrogen Isotopes