title: On the origin of residual dipolar couplings from denatured proteins.
abstract: 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.
authors.affiliation: Department of Physical Sciences, University of Helsinki, Finland, VTT Biotechnology, Espoo, Finland.
authors.forename: Martti
authors.initials: M
authors.lastname: Louhivuori
authors.forename: Kimmo
authors.initials: K
authors.lastname: Pääkkönen
authors.forename: Kai
authors.initials: K
authors.lastname: Fredriksson
authors.forename: Perttu
authors.initials: P
authors.lastname: Permi
authors.forename: Juhani
authors.initials: J
authors.lastname: Lounila
authors.forename: Arto
authors.initials: A
authors.lastname: Annila
mesh_terms: D016880:Anisotropy; D003198:Computer Simulation; D008956:Models, Chemical; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011489:Protein Denaturation; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins