Protein aggregation and gel formation studied with scattering methods and computer simulations |
| |
| Affiliation: | 1. College of Light Industry and Food Sciences, South China University of Technology, 510640 Guangzhou, China;2. LUNAM Université du Maine, IMMM UMR-CNRS 6283, Polymères, Colloïdes et Interfaces, 72085 Le Mans Cedex 9, France;1. Department of Food Science, Engineering and Technology, College of Agriculture & Natural Resources, University of Tehran, Karaj Campus, Karaj, Iran;2. Transfer Phenomena Laboratory (TPL), Controlled Release Center, Department of Food Science, Technology and Engineering Faculty of Agricultural Engineering and Technology, University of Tehran, Karaj Campus, Karaj, Iran;3. Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran;4. Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran;2. Department of Structure and Material Design, Swedish Institute for Food and Biotechnology, SIK, Göteborg, Sweden;3. SuMo BIOMATERIALS, VINN Excellence Center, Chalmers University of Technology, Göteborg, Sweden;4. Department of Applied Surface Chemistry, Chalmers University of Technology, Göteborg, Sweden;5. Mathematical Sciences, Chalmers University of Technology, and the University of Gothenburg, Göteborg, Sweden;1. Le Mans Université, IMMM UMR-CNRS 6283, Polymères, Colloïdes et Interfaces, 72085 Le Mans, cedex 9, France;2. Université de Tunis El Manar, Faculté des Sciences de Tunis, LR99ES16 Laboratoire Physique de la Matière Molle et de la Modélisation Électromagnétique, 2092, Tunis, Tunisia;1. Department of Food Science, Aarhus University, Blichers Allé 20, DK-8830, Tjele, Denmark;2. AKV Langholt, Gravsholtvej 92, 9310, Vodskov, Denmark;3. KMC, Herningvej 60, 7330, Brande, Denmark |
| |
| Abstract: | We review recent scattering experiments on the reversible and irreversible aggregation and gelation of globular proteins. Globular proteins are compact with a well-defined structure in the native state, but are not perfect spheres and the details of the interaction between proteins may be intricate involving for instance specific binding sites. Nevertheless, it turns out that often the structure of globular protein aggregates and gels can be understood by treating them as spherical colloids with relatively simple interaction potentials. Computer simulations of interacting hard spheres give detailed structural information that can be used to understand some aspects of protein aggregation and gel formation. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
