Lorentz JÄNTSCHI (lori) works ?id=183
- [id] => 183
- [recorddate] => 2008:10:17:11:02:12
- [lastupdate] => 2008:10:17:11:02:12
- [type] => conference
- [place] => Plovdiv, Bulgaria
- [subject] => mathematics - modeling; mathematics - number theory; mathematics - statistics; medicine - informatics
- [relatedworks] =>
- 2 (average):
- Distribution fitting 3. Analysis under normality assumption, ?id=197

- [file] => ?f=183
- [mime] => application/pdf
- [size] => 3482713
- [pubname] => Fifth International Conference of Applied Mathematics and Computing
- [pubinfo] => University of Chemical Technology and Metallurgy Sofia & Technical University of Plovdiv
- [pubkey] => Invited lecture, presented on August 14, from 11.30 to 12.00
- [workinfo] => Proc Int Conf Appl Math Comput 2008 5(1), p. 84
- [year] => 2008
- [title] => Analysis of collagen type I chains
- [authors] => Sorana D. BOLBOACĂ, Lorentz JÄNTSCHI
- [abstract] =>

Collagen type I, consists of a heterotrimer of two α1(I) and one α2(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 α 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.
- [keywords] => Correlation; Amino Acids Sequence; Chains of Type I Collagen
- [acknowledgment] => CNCSIS Romania supports the research through project AT93/2007.