oligomeric protein

oligomeric protein

[ə‚lig·ə′mer·ik ′prō‚tēn]
(biochemistry)
A protein composed of two or more polypeptide chains.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
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The model system of primary monocyte-derived macrophages also responded to activation only with certain viral oligomeric protein structures and their IC.
Therefore, viral oligomeric proteins might be one of many potential macrophage polarization factors.
Another example of oligomeric proteins are amyloid beta (A[beta]) aggregates that are involved in the pathogenesis of AD.
Skin biopsies showed that the fresolimumab-induced rapid decline in mRSS was accompanied by a sharp drop in skin biomarkers of TGF-beta activity, including expression of the genes thrombospondin-1, cartilage oligomeric protein, and connective tissue growth factor.
The former is generally an Oligomeric protein, the later a monomeric iron-sulfur flavoproein[11].
An acidic oligomeric protein (COMP) detected only in cartilage, " Journal of Biological Chemistry, vol.
The present study confirms that the two-state irreversible model, built especially on experimental examinations on small globular proteins will hold true for larger oligomeric proteins as well [33].
In particular, the emission characteristics of tryptophan residues in proteins may provide a convenient mechanism with which to investigate changes in the conformation/structure of proteins that result from a variety of factors, such as substrate/ligand binding, association/dissociation of subunits in oligomeric proteins, and unfolding [21].
In this section, square fluctuations of both monomeric and oligomeric proteins based on a large set of slow modes and the highest modes are compared for a deeper analysis of interfaces.
In 2007, Carugo [6] proposed a method which is able to predict the quaternary structural type of hetero oligomeric proteins. Levy [7] proposed the PiQSi to get the annotations of about 15,000 proteins in PDB, which can be used as the benchmark dataset to test the quality of a method to predict the quaternary structure type.
The endoplasmic reticulum contains a unique pathway for the folding and retention of glycoproteins, central to which is calnexin (7) which assists in the initial folding of glycoproteins, retains transport-incompetent misfolded glycoproteins, and may function in assembling of oligomeric proteins in the ER (8).