title: Protein structure and interactions in the solid state studied by small-angle neutron scattering.
abstract: Small-angle neutron scattering (SANS) is uniquely qualified to study the structure of proteins in liquid and solid phases that are relevant to food science and biotechnological applications. We have used SANS to study a model protein, lysozyme, in both the liquid and water ice phases to determine its gross-structure, interparticle interactions and other properties. These properties have been examined under a variety of solution conditions before, during, and after freezing. Results for lysozyme at concentrations of 50 mg mL(-1) and 100 mg mL(-1), with NaCl concentrations of 0.4 M and 0 M, respectively, both in the liquid and frozen states, are presented and implications for food science are discussed.
authors.affiliation: NIST Center for Neutron Research, NIST, Gaithersburg, MD 20899, USA.
authors.forename: Joseph E
authors.initials: JE
authors.lastname: Curtis
authors.forename: Arnold
authors.initials: A
authors.lastname: McAuley
authors.forename: Hirsh
authors.initials: H
authors.lastname: Nanda
authors.forename: Susan
authors.initials: S
authors.lastname: Krueger
mesh_terms: D017666:Deuterium Oxide; D005502:Food; D005615:Freezing; D009113:Muramidase / Q000737:chemistry*; D033363:Neutron Diffraction; D011487:Protein Conformation; D053838:Scattering, Small Angle; D012965:Sodium Chloride / Q000737:chemistry*; D012996:Solutions; D014867:Water / Q000737:chemistry*
chemical_list: D012996:Solutions; D014867:Water; D012965:Sodium Chloride; D009113:Muramidase; D017666:Deuterium Oxide