Globular Proteins

Globular Proteins

 

crystalline proteins that are easily soluble in water or weak saline solutions; their molecules are close to spherical (the ratio of the sphere’s axes does not exceed 5). Such a molecular structure is determined by the spiralization of the peptide chain and by its dense packing, which is due to the tertiary structure. Many globular proteins exhibit enzymatic activity. Globulins, myoglobin, and ribonuclease are among the important globular proteins. Some proteins, such as actin, exist in both globular and elongated fibrillar form.

References in periodicals archive ?
Scientists at the University of Massachusetts controlled interfacial properties using two globular proteins with widely differing isoelectric points.
The globular proteins fold into complicated sphere-shaped structures held mutually by an arrangement of hydrogen, ionic, hydrophobic, and covalent (disulphide) bonds.
The 1962 Nobel Prize in chemistry went to John Kendrew and Max Perutz "for their studies of the structures of globular proteins.
Results of this project will boost the knowledge related to the first misfolding events leading to AT3 pathological aggregation as well as our understanding on subtle misfolding events triggering protein aggregation of folded globular proteins.
Lorient et al, [34] note that unfolding of the [beta]-Iactoglobuline and [alpha]-lactalbumin by reduction and carboxymethylation S-S bridges also increases the flexibility of the molecules, while thermal denaturation does not seem to significant effects unless the proteins precipitate which case the mobility is greatly reduced; these observations on mobility and flexibility can be easily connected not only to the structure more or less deshirred molecules, but also because the interfacial behavior surfactant properties are best when mobility is higher (flexible proteins such as casein and globular proteins deshirred, pHi, presence of salts, etc.
Their topics include what a polymer molecule looks like, polymers in nature, the physics of high elasticity, globular proteins and folding, the dynamics of polymer fluids, and the mathematics of fractals as complicated polymer structures.
It can be considered as a positive factor for the enhancement of thermo stability of globular proteins.
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.
Enzymes are globular proteins that serve as catalysts for a range of biological and chemical reactions and have a variety of applications.
Binding (non-covalent) and grafting (covalent) methods make it possible to attach globular proteins to polymer surfaces.
Proteins can be divided into two major categories: fibrous proteins and globular 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.