globular protein


Also found in: Dictionary, Thesaurus, Encyclopedia, Wikipedia.

glob·u·lar pro·tein

any protein soluble in water, usually with added acid, alkali, salt, or ethanol, and roughly so classified (albumins, globulins, histones, and protamines), in contrast to fibrous protein.

glob·u·lar pro·tein

(globyū-lăr prōtēn)
Any protein soluble in water, usually with added acid, alkali, salt, or ethanol, and roughly so classified (albumins, globulins, histones, and protamines).

globular protein

Any protein readily soluble in a weak salt solution. GLOBULINS are globular proteins. Also known as eublobulins.

globular protein

a type of PROTEIN, folded and twisted into a tertiary structure.
References in periodicals archive ?
0])) was plotted against the logarithm of the MW of globular proteins and purified cardiac troponin standards.
Several implications of the epitope analysis we have performed argue against hcTnI being globular, at least in the uncomplexed form that was used for immunization: (a) all 16 anti-hcTnI mAbs recognized a continuous epitope markedly; this contrasts with the observation that most mAbs to globular proteins show a conformation-dependent recognition [12] and, therefore, do not react with short peptides; (b) several helices of hcTnI are antigenic, which means that they are probably exposed to the solvent and not packed together as in globular proteins; and (c) we observed that regions connecting the predicted helices of hcTnI are not antigenic; this is in sharp contrast with the fact that turn regions in globular proteins are generally antigenic.
In natural states, proteins generally exist in two form fibrous proteins and globular proteins [138].
NasdaqGS: VARI) announced today the release of ProSEC(TM) 300S, a new size exclusion chromatography column designed for the accurate and precise analysis of globular proteins in the pharmaceutical and bioscience industries.
The special surface technology of ProSEC columns reduces protein interactions, resulting in high sample recovery and reliable analysis of a wide range of globular proteins.
The molecular backbones of globular proteins have an intricates structure.
Force to Unbind Ligand-Receptor Complexes and the Internal Rigidity of Globular Proteins Probed by Single-Molecule Force Spectroscopy
s] than globular proteins with a comparable relative molecular mass ([M.