Protein structure and interactions in the solid state studied by small-angle neutron scattering

Joseph E. Curtis; Arnold McAuley; Hirsh Nanda; Susan Krueger

doi:10.1039/C2FD20027A

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Faraday Discussions

Issue 1, 2012

Discussion summary and research papers, in physical chemistry, chemical physics and biophysical chemistry.

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Protein structure and interactions in the solid state studied by small-angle neutron scattering

Joseph E. Curtis,^a Arnold McAuley,^b Hirsh Nanda^a and Susan Krueger*^a

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NIST Center for Neutron Research, NIST, Gaithersburg, USA
E-mail: susan.krueger@nist.gov

Department of Analytical and Formulation Sciences, Amgen Inc., One Amgen Center Drive, Thousand Oaks, USA

Faraday Discuss., 2012,158, 285-299

DOI: 10.1039/C2FD20027A
Received 17 Feb 2012, Accepted 05 Apr 2012
First published online 01 Aug 2012

This article is part of themed collection: Soft Matter Approaches to Structured Foods

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Abstract
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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.

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