Literature DB >> 3657197

Number of ways of joining SH groups to form multi-peptide chain proteins.

Z X Wang1, M Ju, C L Tsou.   

Abstract

The expression for the total number of isomeric structures formed upon oxidation of SH groups has previously been correctly obtained for single chain proteins only. Expressions have now been obtained for molecules consisting of 2 and 4 peptide chains of the types A2 and A2B2. The latter type is particularly important as exemplified by the immunoglobulins and the insulin receptor. For the oxidation of insulin A chain with 4 SH groups, the total number of isomeric A2 structures is 59--this is different to all the values previously reported. Lack of consideration of symmetry problems probably accounts for the erroneous results obtained by earlier workers for the number of ways of randomly joining two identical chains. The total number of isomeric structures formed from the oxidation of two light and two heavy chains with 5 and 11 SH groups respectively of the human immunoglobulin GI has been found to be 4.8 X 10(16).

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Year:  1987        PMID: 3657197     DOI: 10.1016/s0022-5193(87)80117-0

Source DB:  PubMed          Journal:  J Theor Biol        ISSN: 0022-5193            Impact factor:   2.691


  2 in total

1.  The insulin A and B chains contain structural information for the formation of the native molecule. Studies with protein disulphide-isomerase.

Authors:  J G Tang; C L Tsou
Journal:  Biochem J       Date:  1990-06-01       Impact factor: 3.857

2.  Formation of native insulin from the scrambled molecule by protein disulphide-isomerase.

Authors:  J G Tang; C C Wang; C L Tsou
Journal:  Biochem J       Date:  1988-10-15       Impact factor: 3.857

  2 in total

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