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Analysis of Collagen Type I Chains

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CONTRIBUTORS:
  Author Sorana D. BOLBOACA (Iuliu Hatieganu University of Medicine and Pharmacy Cluj-Napoca)
  Author Lorentz JÄNTSCHI (Technical University of Cluj-Napoca)
CONFERENCE NAME:
  Fifth International Conference of Applied Mathematics and Computing
CONF. LOCATION: Plovdiv, Bulgaria
CONFERENCE YEAR: 2008
PUB TYPE: Conference Presentation
SUBJECT(S): mathematics - modeling; mathematics - number theory; mathematics - statistics; medicine - informatics
DISCIPLINE: Mathematics
HTTP: http://lori.academicdirect.org/works/?f=198
LANGUAGE: English
PUB ID: 103-445-898 (Last edited on 2008/10/17 02:48:36 GMT-6)
SPONSOR(S):
 
ABSTRACT:
Collagen type I, consists of a heterotrimer of two á1(I) and one á2(I) chains, is the most common form of fibrillar collagen, being a major constituent of bone and skin. The research presents a correlation analysis of amino acids within and between collagen types I chains in the same specie and in different species. The collagen type I chains from the following species were included into analysis: Rattus norvegicus (Orjel at al., 2006), Bos taurus (Shirai et al., 1998), Danio rerio (Howden, 2007), Canis lupus (Lowe et al., 2003), and Homo sapiens (Strausberg et al., 2002). The correlation obtained were analyzed in accordance with the distribution of amino acids in the collagen type I chains. A perfect correlation (r = 1) was obtained between species on the same á chain for cysteine, tryptophan, tyrosine, and lysine. The highest correlation on different collagen type I chains (r =0.763) of the same species was obtained for Canis lupus.
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