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Patel, Siddharth and Indu, S and Ramakrishnan, C and Varadarajan, Raghavan (2013) PROTEIN DISULFIDE ANALYSIS AND DESIGN. In: Conference on Biomolecular Forms and Functions - A Celebration of 50 Years of the Ramachandran Map, JAN, 2013, Indian Inst Sci, Bangalore, INDIA, pp. 296-311.

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The significant contribution of naturally occurring disulfide bonds to protein stability has encouraged development of methods to engineer non-native disulfides in proteins. These have yielded mixed results. We summarize applications of the program MODIP for disulfide engineering. The program predicts sites in proteins where disulfides can be stably introduced. The program has also been used as an aid in conformational analysis of naturally occurring disulfides in a-helices, antiparallel and parallel beta-strands. Disulfides in a-helices occur only at N-termini, where the first cysteine residue is the N-cap residue of the helix. The disulfide occurs as a CXXC motif and can possess redox activity. In antiparallel beta-strands, disulfides occur exclusively at non-hydrogen bonded (NHB) registered pairs of antiparallel beta-sheets with only 1 known natural example occurring at a hydrogen bonded (HB) registered pair. Conformational analysis suggests that disulfides between HB residue pairs are under torsional strain. A similar analysis to characterize disulfides in parallel beta-strands was carried out. We observed that only 9 instances of cross-strand disulfides exist in a non-redundant dataset. Stereochemical analysis shows that while tbe chi(square) angles are similar to those of other disulfides, the chi(1) and chi(2) angles show more variation and that one of tbe strands is generally an edge strand.

Item Type: Conference Proceedings
Additional Information: Copyright for this article belongs to the WORLD SCIENTIFIC PUBL CO PTE LTD, PO BOX 128 FARRER RD, SINGAPORE 9128, SINGAPORE
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 14 Jul 2014 09:03
Last Modified: 16 Jul 2014 05:08
URI: http://eprints.iisc.ac.in/id/eprint/49489

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