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Is Amino Acids Hydrophobicity a Matter of Scale?

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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 TITLE:
  Recent Advances in Synthesys & Chemical Biology VI
CONF. LOCATION: None
YEAR: 2007
PUB TYPE: Conference Paper
SUBJECT(S): chemistry - biochemistry; mathematics - modeling; mathematics - number theory; mathematics - probability theory; medicine - informatics; research - evaluation
DISCIPLINE: Biochemistry
HTTP: http://lori.academicdirect.org/works/?f=168
LANGUAGE: English
PUB ID: 103-439-281 (Last edited on 2007/12/20 03:47:39 US/Mountain)
SPONSOR(S):
 
ABSTRACT:
Hydrophobic or hydrophilic character of an amino acid, the property important in protein structure and protein-protein interactions, is one of the most studied properties of amino-acids. To date, many hydrophobicity scales have been reported, the differences between them being significant: Janin (1979) and Kyte and Doolittle (1982) classify cistein as the most hydrophobic while Wolfenden et al. (1981) or Rose et al. (1985) do not. The aim of the research was to perform a structural modelling analysis of amino acids hydrophobicity in order to identify and characterize if there exists a relationship between the structure and the property, and to quantify these relationships.
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