Analysis of disulfide bonds in protein structures
نویسندگان
چکیده
منابع مشابه
Disulfide bonds, their stereospecific environment and conservation in protein structures.
We studied the specificity of the non-bonded interaction in the environment of 572 disulfide bonds in 247 polypeptide chains selected from the Protein Data Bank. The preferred geometry of interaction of peptide oxygen atoms is along the back of the two covalent bonds at the sulfur atom of half cystine. With aromatic residues the geometries that direct one of the sulfur lone pair of electrons in...
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The prevailing view is that disulfide bonds have been added during evolution to enhance the stability of proteins that function in a fluctuating cellular environment. However, recent evidence indicates that disulfide bonds can be more than inert structural motifs. The function of some secreted soluble proteins and cell-surface receptors is controlled by cleavage of one or more of their disulfid...
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متن کاملPatterns in the sequence context of protein disulfide bonds by
Disulfide bonds play an important role in the structural stability of the proteins that contain them. Yet, little is known about the specificity with which they are formed. To address this, a representative set of disulfide bonds from nonhomologous eukaryotic polypeptides was created. The amino acid sequences flanking these disulfide bonds were searched for conserved patterns that may reflect r...
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ژورنال
عنوان ژورنال: Journal of Thrombosis and Haemostasis
سال: 2010
ISSN: 1538-7933
DOI: 10.1111/j.1538-7836.2010.03894.x