tropocollagen


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Related to tropocollagen: collagen fibers

tropocollagen

 [tro″po-kol´ah-jen]
the basic structural unit of collagen; it is a helical structure consisting of three polypeptide chains coiled around each other to form a spiral and stabilized by interchain bonds.
Miller-Keane Encyclopedia and Dictionary of Medicine, Nursing, and Allied Health, Seventh Edition. © 2003 by Saunders, an imprint of Elsevier, Inc. All rights reserved.

tro·po·col·la·gen

(trō'pō-kol'ă-jen),
The fundamental units of collagen fibrils, consisting of three helically arranged polypeptide chains.
Farlex Partner Medical Dictionary © Farlex 2012

tropocollagen

(trō′pə-kŏl′ə-jən, trŏp′ə-)
n.
The molecular component of a collagen fibril, consisting of three polypeptide chains coiled around each other.
The American Heritage® Medical Dictionary Copyright © 2007, 2004 by Houghton Mifflin Company. Published by Houghton Mifflin Company. All rights reserved.

tro·po·col·la·gen

(trō'pō-kol'ă-jĕn)
The fundamental units of collagen fibrils, consisting of three helically arranged polypeptide chains.
Medical Dictionary for the Health Professions and Nursing © Farlex 2012
References in periodicals archive ?
Once outside the cell, the collagen propeptides are cleaved in the extracellular space and tropocollagen is formed by the enzymatic action of procollagen peptidase (as discussed in [29]).
Based on DSC data, particularly the changes associated with Tc and Td and the changes in the infrared rations 840/850 and 505/511 [cm.sup.-1], and the fact that in composites tropocollagen structure was maintained, a model for anionic collagen:P(VDF/TrFE) interaction was proposed and shown in Figure 8.
The results show that under the appropriate conditions anionic collagen: P(VDF/TrFE) composites with ratios in the range from 4:1 to 1:1 may be conveniently prepared in the form of membranes without loss of tropocollagen secondary structure and characterized by the macromolecular interaction suggested by infrared and DSC data.
The salt soluble collagen is basically uncross-linked tropocollagen random coils, which is testified by the CD spectra that clearly shows the random coil orientation of the isolated collagen (Fig.
Col type I was obtained using an enzymatic method to remove the nonhelical ends (telopeptides) of the triple helix region to result in a nonimmunogenic polymer of 308 kDa, similar to the molecular weight of tropocollagen (300 kDa), as we previously showed [21].
During genesis of collagen fibers, three parallel "left-handed" PPII helical [alpha]-chains "self-assemble" around each other with a one amino acid stagger in a "right-handed" fashion to form a right-handed triple helix referred to as a tropocollagen molecule [18-23].
The basic structural unit is called tropocollagen, which has a molecular weight of [approximately]300,000 and consists of three polypeptide chains of the same size (1000 amino acid residues).
Postlethwaite and Kang (1976) reported that native tropocollagen, as well as peptide fragments, derived from the protein by degradation with CNBr, pepsin, or bacterial collagenase was chemotactic for monocytes.
Soft Tissues, Collagen, and Iridescence.--Type I collagen is the most abundant protein in animal soft tissues and is composed of banded fibers (tropocollagens) with a transverse periodicity.