Proteins and other biomolecules undergo a dynamic transition to a glass-like solid state with small atomic fluctuations. This dynamic transition can inhibit biological function and alter their material properties.Institute of Food Technologists; Illinois Department of Agricultur
The stability of biologically produced pharmaceuticals is the limiting factor to various application...
Water holding (WH) of soy protein gels was investigated to identify which length scales are most con...
The stability of biologically produced pharmaceuticals is the limiting factor to various application...
The effects of moisture and thermal denaturation on the solid-state structure and molecular mobility...
The effects of moisture and thermal denaturation on the solid-state structure and molecular mobility...
We report a multitechnique study of structural organization and molecular mobility for soy glycinin ...
Hydrated soy-proteins display different macroscopic properties below and above approximately 25%mois...
Hydrated soy-proteins display different macroscopic properties below and above approximately 25% moi...
The 7S/11S glycinin equilibrium as found in Lakemond et al. (J. Agric. Food Chem. 2000, 48, xxxx-xxx...
Formation and structure of glycinin gels were studied in relation to protein conformation for two pH...
This study describes the relationship between the solubility of glycinin, a major soy protein, and i...
The thermal denaturation behaviour of glycinin solutions has been studied in situ as a function of i...
key words: soy protein; glycinin; thermal stability; pH; ionic strength;genetic variant; solubility;...
Abstract Background Protein instability remains the main factor limiting the development of protein ...
<p>key words: soy protein; glycinin; thermal stability; pH; ionic strength;genetic variant; so...
The stability of biologically produced pharmaceuticals is the limiting factor to various application...
Water holding (WH) of soy protein gels was investigated to identify which length scales are most con...
The stability of biologically produced pharmaceuticals is the limiting factor to various application...
The effects of moisture and thermal denaturation on the solid-state structure and molecular mobility...
The effects of moisture and thermal denaturation on the solid-state structure and molecular mobility...
We report a multitechnique study of structural organization and molecular mobility for soy glycinin ...
Hydrated soy-proteins display different macroscopic properties below and above approximately 25%mois...
Hydrated soy-proteins display different macroscopic properties below and above approximately 25% moi...
The 7S/11S glycinin equilibrium as found in Lakemond et al. (J. Agric. Food Chem. 2000, 48, xxxx-xxx...
Formation and structure of glycinin gels were studied in relation to protein conformation for two pH...
This study describes the relationship between the solubility of glycinin, a major soy protein, and i...
The thermal denaturation behaviour of glycinin solutions has been studied in situ as a function of i...
key words: soy protein; glycinin; thermal stability; pH; ionic strength;genetic variant; solubility;...
Abstract Background Protein instability remains the main factor limiting the development of protein ...
<p>key words: soy protein; glycinin; thermal stability; pH; ionic strength;genetic variant; so...
The stability of biologically produced pharmaceuticals is the limiting factor to various application...
Water holding (WH) of soy protein gels was investigated to identify which length scales are most con...
The stability of biologically produced pharmaceuticals is the limiting factor to various application...