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Albany 2019: 20th Conversation - Abstracts

category image Albany 2019
Conversation 20
June 11-15 2019
Adenine Press (2019)

Stoichiometric Constraints in Protein Sequences

About a decade ago, rigorous analyses of structural data of thousands of naturally occurring folded proteins yielded a surprising “margin of life” for stoichiometric composition, i.e. percentage occurrence of individual amino acids, of protein sequences (Mittal et al., 2010; Mittal & Jayaram, 2011a, 2011b). This “margin of life” refers to the lower than expected variances in percentage occurrence of individual amino acids in protein sequences (Mezei, 2011). The concept of “margin of life” is about a decade old now and has been confirmed over a large sequence space for almost all known protein sequences (even in absence of structural data for a large number of sequences). While the earlier work was based on the largest structural dataset at that time, in this work further explorations on compositional constraints for known protein sequences are presented on the largest dataset analyzed till date. The relationships between peptide-bonded pairs and triplets of amino acids, in about half-a-million protein sequences, with their various physico-chemical properties and individual proportions (of the peptide-bonded pairs and triplets) are explored. While having profound evolutionary implications towards our insights into occurrence of naturally occurring protein sequences, the results discussed also promise to serve as guide for creating stable and structurally controlled and/or “disordered” designer proteins.

References

    Mittal, A., Jayaram, B., Shenoy, S. R. & Bawa, T. S. (2010). A stoichiometry driven universal spatial organization of backbones of folded proteins: Are there Chargaff’s rules for protein folding? J. Biomol. Struct. Dyn. 28: 133-142.

    Mittal, A. & Jayaram, B. (2011a). Backbones of Folded Proteins Reveal Novel Invariant Amino Acid Neighborhoods. J. Biomol. Struct. Dyn. 28: 443-454.

    Mittal, A. & Jayaram, B. (2011b). The Newest View on Protein Folding: Stoichiometric and Spatial Unity in Structural and Functional Diversity. J. Biomol. Struct. Dyn. 28: 669-674.

    Mezei, M. (2011). Discriminatory Power of Stoichiometry-Driven Protein Folding? J. Biomol. Struct. Dyn. 28: 625-626.

Aditya Mittal

Kusuma School of Biological Sciences
IIT Delhi
Hauz Khas
New Delhi 110016

Ph: (91) 11-26591052
Email: amittal@bioschool.iitd.ac.in