title: Analysis of factors that induce cysteine bonding state.
abstract: Regarding the fact that the protein structure is principally encoded in its sequence, investigating the bonding state of cysteine has gained a great deal of attention due to its significance in the formation of protein structure. Due to lack of evident influence of free cysteines on the protein structure, it may be expected that only half-cystines convey encoded information. The results obtained from the analysis of amino acid distribution in proximity of both states of cysteines explicitly indicated that perquisite information for inducing cysteine bonding state is present even in the flanking amino acid sequences of free cysteines.
authors.affiliation: Department of Biophysics, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran. [corrected]
authors.forename: Somayyeh
authors.initials: S
authors.lastname: Hoseini
authors.forename: Mina
authors.initials: M
authors.lastname: Jahandideh
authors.forename: Afsaneh
authors.initials: A
authors.lastname: Hoseini
authors.forename: Ali Salehzadeh
authors.initials: AS
authors.lastname: Yazdi
authors.forename: Zahra
authors.initials: Z
authors.lastname: Karami
authors.forename: Parviz
authors.initials: P
authors.lastname: Abdolmaleki
authors.forename: Mohammad Ali
authors.initials: MA
authors.lastname: Rezaei
authors.forename: Samad
authors.initials: S
authors.lastname: Jahandideh
authors.forename: Ebrahim Barzegari
authors.initials: EB
authors.lastname: Asadabadi
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D019295:Computational Biology / Q000379:methods*; D003198:Computer Simulation; D003545:Cysteine / Q000737:chemistry*; D030562:Databases, Protein; D004220:Disulfides; D008968:Molecular Conformation; D015394:Molecular Structure; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D020539:Sequence Analysis, Protein; D012984:Software
chemical_list: D000596:Amino Acids; D004220:Disulfides; D011506:Proteins; D003545:Cysteine