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 ?
The majority of the literature related to the electrostatic adsorption of proteins onto microparticles focussed on globular proteins specially using whey proteins ([beta]-lactoglobulin ~65% of whey total proteins, 18.4KDa) according to DOHERTHY et al.
Globular proteins are usually curled up so that the hydrophobic R regions are centered in the molecule to avoid the polar environment around them, while the hydrophilic R group is located on the surface of the molecule.
Atsushi, Thermostability and aliphatic index of globular proteins. J.
Globular proteins may have a combination of the above types of structures and are mostly clumped into a shape of a ball.
Scientists at the University of Massachusetts controlled interfacial properties using two globular proteins with widely differing isoelectric points: lactoferrin (pI [approximately equal to] 8.5) and beta-lactoglobulin (pI [approximately equal to] 5).
The globular proteins fold into complicated sphere-shaped structures held mutually by an arrangement of hydrogen, ionic, hydrophobic, and covalent (disulphide) bonds.
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.
Lesser, "Hydrophobicity of amino acid residues in globular proteins," Science, vol.
The 1962 Nobel Prize in chemistry went to John Kendrew and Max Perutz "for their studies of the structures of globular proteins." In the same year, the prize in physiology and medicine went to Francis Crick, James Watson, and Maurice Wilkins "for their discoveries concerning the molecular structure of nucleic acids and its significance for information transfer in living material
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.).