Publication year: 2011 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 16 February 2011
Dylan T., Murray , Yuanting, Lu , T.A., Cross , J.R., Quine
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. Graphical abstract
*Graphical abstract:**Research highlights:*? SSNMR orientational restraints from PISEMA are used to find the structure of a kinked alpha helix. ? For use with orientational restraints, a mathematical model of a kinked alpha helix is presented. ? Orientation of helix segments with respect to B determines torsion angles at the residue between. ? Helix rotation and tilt angles from ssNMR used to determine torsion angle pair in kinked helix
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
Eur Biophys J. 2011 Apr;40(4):447-62
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Geometry of kinked protein helices from NMR data.
Geometry of kinked protein helices from NMR data.
Geometry of kinked protein helices from NMR data.
J Magn Reson. 2011 Feb 16;
Authors: Murray DT, Lu Y, Cross TA, Quine JR
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...
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03-23-2011 05:41 PM
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Geometry of kinked protein helices from NMR data
Linear Mode
