On the origin of residual dipolar couplings from denatured proteins.
Effects of steric obstruction on random flight chains are examined. Spatial probability distributions are elaborated to calculate residual dipolar couplings and residual chemical shift anisotropy, parameters that are acquired by NMR spectroscopy from solutes dissolved in dilute liquid crystals. Calculations yield chain length and residue position-dependent values in good agreement with simulations to provide understanding of recently acquired data from denatured proteins.
Louhivuori
Martti
M
Department of Physical Sciences, University of Helsinki, Finland, VTT Biotechnology, Espoo, Finland.
Pääkkönen
Kimmo
K
Fredriksson
Kai
K
Permi
Perttu
P
Lounila
Juhani
J
Annila
Arto
A
D016880:Anisotropy; D003198:Computer Simulation; D008956:Models, Chemical; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*
D011506:Proteins