1hpn
From Proteopedia
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N.M.R. AND MOLECULAR-MODELLING STUDIES OF THE SOLUTION CONFORMATION OF HEPARIN
Overview
The solution conformations of heparin and de-N-sulphated, re-N-acetylated, heparin have been determined by a combination of n.m.r. spectroscopic and, molecular-modelling techniques. The 1H- and 13C-n.m.r. spectra of these, polysaccharides have been assigned. Observed 1H-1H nuclear Overhauser, enhancements (n.O.e.s) have been simulated using the program NOEMOL, [Forster, Jones and Mulloy (1989) J. Mol. Graph. 7, 196-201] for molecular, models derived from conformational-energy calculations; correlation times, for the simulations were chosen to fit experimentally determined 13C, spin-lattice relaxation times. In order to achieve good agreement between, calculated and observed 1H-1H n.O.e.s it was necessary to assume that the, reorientational motion of the polysaccharide molecules was not isotropic, but was that of a symmetric top. The resulting model of heparin in, solution is similar to that determined in the fibrous state by, X-ray-diffraction techniques [Nieduszynski, Gardner and Atkins (1977) Am., Chem. Soc. Symp. Ser. 48, 73-80].
About this Structure
1HPN is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
N.m.r. and molecular-modelling studies of the solution conformation of heparin., Mulloy B, Forster MJ, Jones C, Davies DB, Biochem J. 1993 Aug 1;293 ( Pt 3):849-58. PMID:8352752
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