globular protein


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globular protein

[′gläb·yə·lər ′prō‚tēn]
(biochemistry)
Any protein that is readily soluble in aqueous solvents.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
Durand, "Salt-induced gelation of globular protein aggregates: Structure and kinetics," Biomacromolecules, vol.
Several globular proteins, including gluten [82], corn protein [44], soy protein [50], and whey protein [83] etc., have been investigated for their film properties.
Because of virtually unlimited possibilities for the variation of an intrinsic molecular balance between the charged and uncharged (hydrophobic) groups on both positive and negative ionic components [1], these substances may offer potentially ideal milieu for any kind of reactant species including biomolecules (e.g., globular proteins), assembled in any kind of (bio)nanodevice.
Elution profiles of globular protein standards (MW varying from 16.9 to 75.0 kDa) and purified cardiac troponin standards (cardiac troponin T-I-C complex, free cTnT, cTnI, and TnC) were determined.
Some areas discussed include gelation and thickening with globular proteins at low temperatures, comparison of thermal and nontheraml characterization of bioglasses, high-pressure treatment effects on food proteins of animal origin, novel techniques for soybean processing, and rheological properties of liquid foods processed in a continuous-flow high-pressure throttling system.
Globular proteins are widely used in the food industry to facilitate the formation and stabilization of foam [3].
In view of the inherent instability of most globular proteins (Somero, 1995; Hochachka and Somero, 2002) and the lack of detectable protein turnover in these embryos (Clegg, 1997; Tanguay et al., 2004), one can assume that at least some globular proteins are indeed unfolding, but that this does not lead to irreversible aggregation.
Many globular proteins, including enzymes, exhibit biological activity.
Proteins can be divided into two major categories: fibrous proteins and globular proteins. A fibrous protein has polypeptide chains arranged in long strands and/or sheets.
Later, when the first globular proteins were finally solved by X-ray crystallography, they revealed that the alpha helix was, in fact, a widespread motif in the folding of many proteins.
The BIAPD can be used in conjunction with Brookhaven's ZetaPALS instruments to take measurements of small globular proteins, micelles, microemulsions, superfine inorganic oxides, metal particles and hydrated salt ions.