Exploring Non-covalent Interactions by Jet-Cooled Electronic …
81
other biologically relevant molecules in the gas phase. However, the major challenge
is to extend this study to the gas phase spectroscopy of larger peptides with a significant number of amino acid residues and still acquiring meaningful information on
the non-covalent interactions present there as well as their structures. Although the
presence of the multiple numbers of N-H and C=O groups in larger peptides can
broaden the IR spectra, it will be possible to have isotope labeling of particular N-H
or C=O group to probe the specific interaction present in the system. Furthermore,
state-of-the-art supercomputing facilities can handle the quantum chemical calculations of the large conformational landscape of the larger peptides and hence aid
the interpretation of the structures observed in the experiment. In the theoretical
front, it is also necessary to develop a better model to improve the calculation of the
scaling factors to correct the harmonic frequencies obtained from the calculations as
anharmonic frequency calculations are computationally expensive.
Acknowledgements We would like to thank our graduate students, postdocs, and collaborators
who have contributed to the results from our laboratory, discussed in this chapter. Financial support
received from Indian Institute of Science Education and Research Pune, Department of Science
and Technology, India (Grant No. SR/S1/PC/0054/2010), and Science and Engineering Research
Board, India (Grant No. EMR/2015/000486) is gratefully acknowledged.
References
1. C.B. Anfinsen, Science 181, 223–230 (1973)
2. J.L. Finney, D.D. Eley, Philos. Trans. R. Soc. B 278, 3–32 (1977)
3. D. Hornby, Hydrogen Bonding in Biological Structures (Springer, Berlin, 1991)
4. A. Karshikoff, Non-covalent Interactions in Proteins (World Scientific, 2006)
5. W. Saenger, Annu. Rev. Biophys. Biophys. Chem. 16, 93–114 (1987)
6. R. Wolfenden, L. Andersson, P.M. Cullis, C.C.B. Southgate, Biochemistry 20, 849–855 (1981)
7. E.A. Meyer, R.K. Castellano, F. Diederich, Angew. Chem. Int. Ed. 42, 1210–1250 (2003)
8. L.M. Salonen, M. Ellermann, F. Diederich, Angew. Chem. Int. Ed. 50, 4808–4842 (2011)
9. W. Saenger, Principles of Nucleic Acid Structure (Springer-Verlag, New York, 1984)
10. G.R. Desiraju, T. Steiner, The Weak Hydrogen Bond in Structural Chemistry and Biology
(Oxford University Press, New York, 1999)
11. J.W. Steed, J L. Atwood, Supramolecular Chemistry (Wiley, New York, 2000)
12. G.R. Desiraju, Angew. Chem. Int. Ed. 46, 8342–8356 (2007)
13. C.A. Hunter, Chem. Soc. Rev. 23, 101–109 (1994)
14. G.A. Jeffrey, An Introduction to Hydrogen Bonding (Oxford University Press, New York,
1997)
15. S. Scheiner, Hydrogen Bonding: A Theoretical Perspective (Oxford University Press, New
York, 1997)
16. E. Arunan, G.R. Desiraju, R.A. Klein, J. Sadlej, S. Scheiner, I. Alkorta, D.C. Clary, R.H.
Crabtree, J.J. Dannenberg, P. Hobza, Pure Appl. Chem. 83, 1637–1641 (2011)
17. T. Ebata, A. Fujii, N. Mikami, Int. Rev. Phys. Chem. 17, 331–361 (1998)
18. G.R. Desiraju, Angew. Chem. Int. Ed. 34, 2311–2327 (1995)
19. A. Chand, H.S. Biswal, J. Indian Inst. Sci. 100, 77–100 (2020)
20. H.S. Biswal, S. Bhattacharyya, A. Bhattacherjee, S. Wategaonkar, Int. Rev. Phys. Chem. 34,
99–160 (2015)
81
other biologically relevant molecules in the gas phase. However, the major challenge
is to extend this study to the gas phase spectroscopy of larger peptides with a significant number of amino acid residues and still acquiring meaningful information on
the non-covalent interactions present there as well as their structures. Although the
presence of the multiple numbers of N-H and C=O groups in larger peptides can
broaden the IR spectra, it will be possible to have isotope labeling of particular N-H
or C=O group to probe the specific interaction present in the system. Furthermore,
state-of-the-art supercomputing facilities can handle the quantum chemical calculations of the large conformational landscape of the larger peptides and hence aid
the interpretation of the structures observed in the experiment. In the theoretical
front, it is also necessary to develop a better model to improve the calculation of the
scaling factors to correct the harmonic frequencies obtained from the calculations as
anharmonic frequency calculations are computationally expensive.
Acknowledgements We would like to thank our graduate students, postdocs, and collaborators
who have contributed to the results from our laboratory, discussed in this chapter. Financial support
received from Indian Institute of Science Education and Research Pune, Department of Science
and Technology, India (Grant No. SR/S1/PC/0054/2010), and Science and Engineering Research
Board, India (Grant No. EMR/2015/000486) is gratefully acknowledged.
References
1. C.B. Anfinsen, Science 181, 223–230 (1973)
2. J.L. Finney, D.D. Eley, Philos. Trans. R. Soc. B 278, 3–32 (1977)
3. D. Hornby, Hydrogen Bonding in Biological Structures (Springer, Berlin, 1991)
4. A. Karshikoff, Non-covalent Interactions in Proteins (World Scientific, 2006)
5. W. Saenger, Annu. Rev. Biophys. Biophys. Chem. 16, 93–114 (1987)
6. R. Wolfenden, L. Andersson, P.M. Cullis, C.C.B. Southgate, Biochemistry 20, 849–855 (1981)
7. E.A. Meyer, R.K. Castellano, F. Diederich, Angew. Chem. Int. Ed. 42, 1210–1250 (2003)
8. L.M. Salonen, M. Ellermann, F. Diederich, Angew. Chem. Int. Ed. 50, 4808–4842 (2011)
9. W. Saenger, Principles of Nucleic Acid Structure (Springer-Verlag, New York, 1984)
10. G.R. Desiraju, T. Steiner, The Weak Hydrogen Bond in Structural Chemistry and Biology
(Oxford University Press, New York, 1999)
11. J.W. Steed, J L. Atwood, Supramolecular Chemistry (Wiley, New York, 2000)
12. G.R. Desiraju, Angew. Chem. Int. Ed. 46, 8342–8356 (2007)
13. C.A. Hunter, Chem. Soc. Rev. 23, 101–109 (1994)
14. G.A. Jeffrey, An Introduction to Hydrogen Bonding (Oxford University Press, New York,
1997)
15. S. Scheiner, Hydrogen Bonding: A Theoretical Perspective (Oxford University Press, New
York, 1997)
16. E. Arunan, G.R. Desiraju, R.A. Klein, J. Sadlej, S. Scheiner, I. Alkorta, D.C. Clary, R.H.
Crabtree, J.J. Dannenberg, P. Hobza, Pure Appl. Chem. 83, 1637–1641 (2011)
17. T. Ebata, A. Fujii, N. Mikami, Int. Rev. Phys. Chem. 17, 331–361 (1998)
18. G.R. Desiraju, Angew. Chem. Int. Ed. 34, 2311–2327 (1995)
19. A. Chand, H.S. Biswal, J. Indian Inst. Sci. 100, 77–100 (2020)
20. H.S. Biswal, S. Bhattacharyya, A. Bhattacherjee, S. Wategaonkar, Int. Rev. Phys. Chem. 34,
99–160 (2015)