Order Matrix Analysis of Residual Dipolar Couplings Using Singular Value Decomposition

The measurement of anisotropic spin interactions, such as residual dipolar couplings, in partially ordered solutions can provide valuable information on biomolecular structure. While the information can be used to refine local structure, it can make a unique contribution in determining the relative...

Full description

Saved in:
Bibliographic Details
Published in:Journal of magnetic resonance (1997) 1999-06, Vol.138 (2), p.334-342
Main Authors: Losonczi, Judit A, Andrec, Michael, Fischer, Mark W.F, Prestegard, James H
Format: Article
Language:English
Subjects:
anisotropic spin interactions
Anisotropy
barley lectin protein
domain–domain orientation
Hordeum
Hydrogen Bonding
Lectins - chemistry
Mathematics
Nitrogen Isotopes
Nuclear Magnetic Resonance, Biomolecular - methods
Plant Lectins
Protein Conformation
Protein Folding
Saupe order matrix
singular value decomposition
Spin Labels
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The measurement of anisotropic spin interactions, such as residual dipolar couplings, in partially ordered solutions can provide valuable information on biomolecular structure. While the information can be used to refine local structure, it can make a unique contribution in determining the relative orientation of remote parts of molecules, which are locally well structured, but poorly connected based on NOE data. Analysis of dipolar couplings in terms of Saupe order matrices provides a concise description of both orientation and motional properties of locally structured fragments in these cases. This paper demonstrates that by using singular value decomposition as a method for calculating the order matrices, principal frames and order parameters can be determined efficiently, even when a very limited set of experimental data is available. Analysis of 1H–15N dipolar couplings, measured in a two-domain fragment of the barley lectin protein, is used to illustrate the computational method.
ISSN:1090-7807
1096-0856
DOI:10.1006/jmre.1999.1754