CURRICULUM VITAE

Name : S. RAGHOTHAMA

Address : NMR Research Centre, Indian Institute of Science, Bangalore - 560 012, India. Phone: +91-80-2293 3301 (Off.) +91-80-2363 3080 (Res.)

Fax: +91-80-2360 1550 mobile: 9880038337

email : sr@nrc.iisc.ernet.in

Gender : Male

Marital Status : Married

Nationality : Indian

Academic Career : MS - Purdue University, USA (1990). (Thesis: Probing enantiodifferentiation in chiral stationary phases using NMR spectroscopy and molecular modeling, (Guide: Prof. K.B. Lipkowitz).

: Ph.D. – IISc, ,Bangalore. India (1998). (Thesis: Structural motifs in designed synthetic peptides:

NMR characterization) (Guide : Prof. P. Balaram and Prof. C.L.Khetrapal.).

: Post doctoral Research fellow (1998-2000) at University of Sheffield, UK, Protein structure determination using 2D and 3D NMR.

(with Prof. M.P. Williamson).

Positions Held : Chief Research Scientist (2014 - Principal Research Scientist (2007 - 2014)

Senior Scientific Officer (2001 - 2007). at NMR Research Centre, Indian Institute of Science, Bangalore, India. Associated with running and maintenance of National

NMR facility since inception from 1977. Currently houses 7 spectrometers (300 – 800MHz ).

Research Areas : Bio-structures, NMR methods, metabolomics. (Highlights attached)

Teaching : CD301 (Jan.semester every year): ‘Two-dimensional NMR Spectroscopy.’ under Integrated Ph.D programme

in Chemical Sciences Division of Indian Institute of Science.

One semester course on ‘NMR Spectroscopy: Practice and Applications to Biological Systems’. at Centre of

Continuing education (Proficience), Indian Institute of Science. (Since 2004).

Current Projects funded by Govt. : (i) Peptide conformations: Solid state NMR study at

Natural abundance. (by CSIR,Government of India)

(ii) Structural Investigations of Amyloid Peptide Fragments Implicated in Alzheimers Disease. (by DST, India)

Awards / Recognition : Bruker Young Scientist Award for the year 1989.

Elected as Executive committee member of National Magnetic Resonance Society. (2007 - 2013) and

nominated as Treasurer.

Membership of Professional Bodies : Life member - National Magnetic Resonance Society,

Life member - National Academy of Sciences - India. Life member - Indian Peptide Society, India.

Life member - American Peptide Society- USA.

General Proficiency : Cryogenics: Associated with Central Cyrogenics Facility, Indian Institute of Science, Bangalore – 560 012, India.

Computers: Molecular Modeling, NMR structure calculation using commercial softwares.

List of Publications : 90 publications in international journal (see list enclosed)

Research Highlights

S. Raghothama.NMR Research Centre, Indian Institute of Science, Bangalore-560012, India.

NMR analysis of natural and synthetically designed peptides:

NMR spectroscopy is a powerful technique for the study of conformational and structural

aspects of biological molecules. In the use of this methodology various approaches are

possible. Of these, one of the important areas is the study of natural and synthetically

designed peptides which have important roles in controlling biological processes.

Currently scientific investigations are focused on the application of NMR spectroscopy to

conformational and structural aspects of such biomolecules. State of the art NMR

methodologies have been applied for such studies and detailed structural analysis have

been carried out. The use of computer based molecular modeling and structure

calculation have also been made. Listed below are some of these studies carried out, part

of which also form collaborative efforts:

(i) Amyloid peptide fragment analysis.

(ii) Studies oriented towards drug design based on natural and synthetic peptides.

(iii) Applications of recent methodological developments in solid state NMR to

peptide structures at natural abundance.

(iv) Understanding protein folding from synthetic design of specific motifs.

(v) 3D-structure elucidation of proteins and peptides.

(vi) Metabolomics studies on stem cell growth media.

Following are the highlights of some of these projects:

(i) Amyloid peptide fragment metal interaction:

Charged residues in Amyloid A fragments, A16 and A12 were shown to be involved in Aluminium binding rather than the usual histidine residues. NMR structures with and without Aluminium was calculated and binding site identified using modeling. Such studies are useful in inhibiting amyloid formation.

(ii) (a) Conus peptides : Contryphans and its analogs study (Lo-959).

Contryphans, cyclic Cysteine containing peptides, extracted from conus toxins are rich source of molecules towards drug development projects. Aromatic-proline interactions influence on structures is analyzed by detailed NMR experiments. Two independent cis / trans NMR structures were calculated. This is a good example of single molecule binding to multiple receptors.

(b) Obestatin fragments and its mutant analysis:

Three overlapping 13 residue fragments along with its mutants of obese control drug obestatin were characterized by NMR and found that the N-terminal fragment and its mutant which has resistance to proterolytic degradation almost matched the parent peptide activity.

(iii) (a) Natural abundance Solid state NMR of designed -turn tripeptide containing Proline residues - cis/trans distinction.

Solution and solid state peptide structures often differs. Solution NMR resulted in cis and trans forms co-existing in a designed tripeptide (Piv-Pro-Pro-Phe-OMe). Crystal structure of the same also had two forms but both were cis. Hence 13C-CPMAS solid state NMR was carried out which matched that of crystal structures. The study shows the power of solid state NMR

trans b) cis

15N CPMAS

which can be used at natural abundance to derive certain structural features.(b) SSNMR peptide structures: Use of single quantum / double quantum (SQ/DQ) methodology: a tripeptide example.

13C -1H SQDQ (single quantum double quantum) correlation experiment again at natural abundance is well utilized to spread out the limited 1H chemical shifts and at the same time identify long range through space interactions. Use pseudo-proline (Pro) to push equilibrium to cis in-turn design is studied. In the absence of crystal structure, this study showed presence of both cis and trans form in the sequence (Piv- Pro-Pro-Leu-NHMe) in contrast to solution single form. A details analysis was carried out along with other connected peptides with complete assignment obtained from different edited experiments of SSNMR.

(iv) (a) Aromatic interactions in stabilizing -hairpin structures:

Diagnostic ring current shift of aromatic protons in case of Phe-Phe interaction is analyzed. The maintenance of the specific aromatic ring orientation in organic solvents provides evidence for significant stabilizing interaction. (b) Hybrid peptides: insertion of higher homologs of amino acids (-aminoacids)

Hybrid polypeptide backbones are potential candidates in protein mimetics. They provide proteolytically stable sequences, very useful in drug design and delivery. Studies show stable secondary structures with -amino acids. (c) Conformation Switch in designed

peptides:

In this interesting study a simple configuration change in central residue -DVal to LVal allow to analyze independently simultaneous existence both helix and extended-hairpin structures. Such studies are very useful in understanding amyloid formation leading to serious diseases.

LIST OF PUBLICATIONS

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- Protrans cisPro

(S. Raghothama, NMR Research Centre, IISc. Bangalore)

1. Determination of chemical shift anisotropy of molecules in a mixture of two liquid crystals of opposite diamagnetic anisotropies.S. RaghothamaJ. Magn. Reson. 57, 294, (1984).

2. Solvent effects on the structure of benzo(b) selenophene oriented in liquid crystals. N. Suryaprakash, S. Raghothama, C.L.Khetrapal, A.C.Kunwar, M. Baiwir and L.Liabres. J. Organometallic Chemistry, 277, 359, (1984)

3. Solid state and solution conformation of Boc-L-Met-Aib-L-Phe-OMe -turn conformation of a sequence related to an active chemotatic peptide analog. R. Bardi, A.M. Piazzesi, C. Toniolo, P. Antony Raj, S. Raghothama and P.Balaram. Int. J. Peptide Protein Res. 27, 229, (1986).

4. Conformation of the amino terminal tetrapeptide of emerimicins and antiamoebins in solution and in the solid state.

R. Bardi, A.M. Piazzesi, C. Toniolo, P. Antony Raj, S. Raghothama and P.Balaram.

Int. J. Biol. Macromol, 8, 201, (1986).

5. Membrane channel forming polypeptide. Molecular conformation and mitochondrial uncoupling activity of antiamoebin, an -amino-isobutyric acid containing peptide. Manoj K.Das, S. Raghothama and P. Balaram. Biochemistry, 25, 7110, (1986).

6. The r-structure, chemical shift anisotropy and the abnormal orientation of methyldichlorophosphine from NMR spectrum.C.L. Khetrapal, S. Raghothama and N. Suryaprakash.J. Magn. Reson., 71, 140, (1987).

7. Cystine peptides, spectroscopic studies on conformation of a cyclic pentapeptide disulfide.R. Kishore, S. Raghothama and P. Balaram.Int. J. Peptide Protein Res. 29, 381, (1987).

8. Cystine peptides. The Intramolecular antiparallel -sheet conformation of a 20-membered cyclic peptide disulfide.

R. Kishore, S. Raghothama and P. Balaram.Biopolymers, 26, 873, (1987).

9. A 1H NMR study of billirubin IX and solubilisation of cholate micelles. An application of nuclear Overhauser effect.Kasturi Lahiri Puranam, S. Raghothama and P. Balaram.Biochem.Biophys. Acta. 922, 67, (1987).

10. Synthetic peptide models for the redox active disulfide loop of glutaredoxin. Conformational studies.R. Kishore, S. Raghothama and P. BalaramBiochemistry, 27, 2462, (1988).

11. Strong coupling and flip angle dependence of coupling patterns in heteronuclear shift correlation two-dimensional NMR spectra.

V.V. Krishnan, S. Raghothama and Anil Kumar. J. Magn. Reson., 79, 328, (1988).

12. Oriented molecules. C.L. Khetrapal, B.S. Arunkumar and S. Raghothama., in “Nuclear Magnetic Resonance” Ed. G.A.Webb. (Specialist Periodical Reports). The Royal Society of Chemistry, London., 17, (1988).

13. Cyclic cystine peptides. Antiparallel -sheet conformation for the 20 membered ring in Boc-Cys-Val-Aib-Ala-Leu-Cys-NHMe

| | S-------------------------S

Isabella L. Karle, R.Kishore, S. Raghothama and P. Balaram. J. Am. Chem. Soc., 110, 1958 (1988).

14. Simultaneous observation of positive and negative nuclear Overhauser effects in oligopeptide due to segmental motion.

K. Uma, H. Balaram, S. Raghothama and P. Balaram. Biochem. Biophys. Res. Comm. 151, 153, (1988).

15. 13C-NMR studies of discotics. C.L.Khetrapal. S. Raghothama, N. Suryaprakash and A.C. Kunwar. Liquid Crystals, 3, 413, 1988.

16. Conformational analysis of cyclolinopeptide A, a cyclic nonapeptide. Nuclear Overhauser effect and energy minimisation studies.

S. Raghothama, C. Ramakrishnan, D. Balasubramanian and P. Balaram. Biopolymers, 28, 573, (1989).

17. Nuclear magnetic resonance and thermal studies of drug doped dipalmitoyl phosphatidyl choline-H2O systems.

K. Usha Deniz, P.S. parvathanathan, Geetha Datta, C.L. Khetrapal, K.V. Ramanathan, N. Suryaprakash and S. Raghothama. J. Biosci., 15, 117, (1990).

18. Probing enantiodefferentiation using NMR spectroscopy and molecular modeling. S. Raghothama and K.B.Lipkowitz. in ‘magnetic Resonance – Current trends’ ed. C.L. Khetrapal and G.Govil., Narosa Publishing House, New Delhi, pp 197-215, (1991).

19. Enantioselective Binding of Tryptophan by -Cyclodextrin. K.B. Lipkowitz, S. Raghothama and J. Yang. J. Am. Chem. Soc. 114, 1554, (1992).

20. Lysozyme-DPPC interaction in the model membrane, DPPC-H2O. P.S. Parvathanathan, Geetha Datta, E.B. Mirza, Lata Sumanan, K. Usha Deniz, K.V.Ramanathan, S. Raghothama, N. Suryaprakash and C.L. Khetrapal. J. Surface Sci. Technol., 8, 29, (1992).

21. Structural studies of o-Vanillin derivatives and their metal complexes by 1 and 2D NMR.

G.A. Naganagowda, S. Raghothama, B.V. Agarwala and C.L. Khetrapal. Bull. Magn. Reson., 18, 81-84, 1995.

22. A designed -hairpin peptide. Satish K Awasthi, S. Raghothama and P. Balaram. Biochem. Biophys. Res. Comm., 216, 375, (1995).

23. Determination of Aib residue conformation in peptides using diagnostic sidechain-backbone Nuclear Overhauser effects.

S. Raghothama, Manjula Chaddha and P. Balaram. Proc. Natl. Acad. Sci. India., 66 (A) Spl. Issue. 33, (1996).

24. Conformational variability in short acyclic peptides. Stabilisation of multiple -turn structures in organic solvents.

Satish Kumar Awasthi, S. Raghothama and P. Balaram. J. Chem. Soc., perkin Trans. 2, 2701-2706 (1996)

25. Ambidextrous Molecules: Cylindrical peptide structures formed by fusing left and right handed helices.

Arindam Banerjee, SrinivasaRao Raghothama, Isabella L. Karle and Padmanabhan Balaram. Biopolymers, 39, 279-285 (1996).

26. NMR analysis of a conformational trasition in an acyclic peptide. A model system for studying helix unfolding. S. Raghothama, M. Chaddha and P. Balaram. J. Phys. Chem., 100, 19666-19671 (1996).

27. Peptide design. Helix-helix motifs in synthetic sequences. Arindam Banerjee, S. Raghothama and P. Balaram J. Chem. Soc. Perkin Trans. 2, 2087-2094 (1997).

28. Stereochemical analysis of higher , -dialkylglycine containing peptides. Characterisation of local helical conformations at Dipropylglycine residue and

observation of a novel hydrated multiple -turn structure in crystals of a glycine rich peptide.

I.L. Karle, Ramesh Kaul, R. Balaji Rao, S. Raghothama and P. Balaram. J. Am. Chem. Soc., 119, 12048-12054 (1997).

29. Conformational interconversions in peptide -turns. Discrimination between enantiomeric conformations by chiral perturbation.

S. Raghothama, Manjula Chaddha, S. Banumathi, Krishna Ravikumar, D. Velumurugan and P. Balaram. Biopolymers, 45, 191-202, (1998).

30. -hairpin nucleation by Pro-Gly -turns. Comparison of D-Pro-Gly and L-Pro-Gly sequences in an apolar octapeptide.

S. Raghothama, S.K. Awasthi and P. Balaram. J. Che. Soc. Perkin Trans. 2, 137-143 (1998).

31. A designed three stranded -sheet peptide. C.Das, S. Raghothama and P. Balaram. J. Am. Chem. Soc. Communication, 120, 5812, (1998).

32. A four stranded -sheet structure in a designed, synthetic polypeptide. Chittaranjan Das, S. Raghothama, and P. Balaram Chem. Commun., 967-968, (1999)

33. Solution structure of the CBM10 cellulose binding module from Pseudomonas xylanase A.

S. Raghothama, Peter J. Simpson, Lorand Szabo, Tibor Nagy, Harry J. Gilbert, and Michael P. Williamson. Biochemistry, 39 (5), 978-984, (2000).

34. Carbohydrate-binding modules from a thermostable Rhodothermus marinus xylanase: cloning, expression and binding studies.

Maher Abou Hachem, Eva Nordberg Karlsson, Eva Bartonek-Roxa, Srinivasarao Raghothama, Peter J. Simpson, Harry J. Gilbert, Michael P. Williamson and Olle Holst. Biochem. J., 345, 53-60 (2000).

35. Synthetic protein design: Construction of a four stranded -sheet structure and evaluation of its integrity in methanol-water mixtures. Chittaranjan Das, V. Nayak, S. Raghothama and P. Balaram J. Peptide Res. 56, 307-317, (2000).

36. Solvent induced -hairpin to helix conformational transition in a designed peptide. S.K. Awasthi, S.C. Shankaramma, S. Raghothama and P. Balaram Biopolymers, 58, 465-476, (2001).

37. Characterisation of a cellulosome dockerin domain from the anaerobic fungus Piromyces equi

S. Raghothama, Ruth Y. Eberhardt, Peter Simpson, Darran Wigelsworth, Peter White, Geoffrey P. Hazlewood, Tibor Nagy, Harry J. Gilbert & Michael P. Williamson Nature Structure Biology, 8, 775-778, (2001)

38. Clostridium thermocellum Xyn10B carbohydrate –binding module 22-2: The role of conserved amino acids in ligand binding.Hefang Xie, Harry J. Gilbert, Simpson J. Charnock, Gideon J. Davies, Michael P Williamson, Peter J. Simpson, S. Raghothama, Carlos M.G.A. Fontes, Fernando M. V. Dias, Luis M. A. Ferreira, and David N. Bolam.Biochemistry, 40, 9167-9176, (2001).

39. – Hairpins generated from hybrid peptide sequences containing both – and – amino acids.

H.N. Gopi, R.S.Roy. S. Raghothama, I.L. Karle and P. BalaramHelvetica Chimica Acta, 85, 3313- 3330, (2002).

40. Two Novel Hexadepsipeptide with several modified amino acid residues isolated from the fungus Isaria. G. Ravindra, R. S. Ranganyaki, S. Raghothama, M.C. Srinivasan, R.D. Gilardi, I.L. Karle and P. Balaram. Chemistry and Biodiversity, 1, 489-504, (2004).41. hybrid peptides: A polypeptide helix with a central segment containing two consecutive -amino acid residues. R.S. Roy, I.L. Karle, S. Raghothama, and P. Balaram. Proc. Natl. Acad. Sci. (USA), 101, 16476-16482, (2004).

42. NMR structural analysis of a peptide mimic of the bridging sheet of HIV-1 gp120 in methanol and water.

Kausik Chakraborty, P. Shivakumar, S. Raghothama & Raghavan Varadarajan Biochem. J. 390, 573-581, (2005).

43 Tryptophan-containing peptide helices: interactions involving the indole sidechain

R.Mahalakshmi. A. Sengupta, S. Raghothama N. Shamala P. Balaram. J.Peptide Res. 66, 277-296, 2005.

44 Peptide Hairpins with Strand Segments Containing - and - Amino Acid Residues: Cross-Strand Aromatic Interactions of Facing Phe Residues.

R.S.Roy , H.N. Gopi, S. Raghothama, R.D.Gilardi,, I.L.Karle,, P. Balaram Peptide Science (Biopolymers), 80, 787-799, 2005.

45 NMR Analysis of Aromatic Interactions in Designed Peptide - Hairpins.

R. Mahalakshmi, S. Raghothama, P.Balaram. J. Am. Chem. Soc, 128, 1125-1138, 2006.

46 Design of a Peptide Hairpin Containing a Central Three-Residue LoopR. Rai, S. Raghothama, and P. Balaram

J. Am. Chem. Soc. 128, 2675-2681, 2006

47 Hybrid peptide Hairpins Containing - and -Amino Acids: Conformational Analysis of Decapeptides with Unsubstituted --and -Residues at Positions 3and 8.R.S. Roy, H.N. Gopi, S. Raghothama, I.L. Karle, and P. Balaram.Chem. Eur. J. 12, 3295-3302, 2006.

48 Diproline Templates as Folding Nuclei in Designed Peptides. Conformational Analysis of Synthetic Peptide Helices Containing Amino Terminal Pro-Pro Segments R.Rai, S.Aravinda, K.Kanagarajadurai, S.Raghothama, N. Shamala, and P. Balaram. J. Am. Chem. Soc. 128, 7916-7928, 2006.

49 Tryptophan rich peptides: Influence of indole rings on backbone conformation R. Mahalakshmi, A. Sengupta, S.Raghothama, N. Shamala, P. BalaramBiopolymers (Peptide Science), 88, 36-54, 2007

50 Tuning the -Turn segment in Designed Peptide -Hairpins: Construction of a Stable Type I’ -Turn Nucleus and Hairpin-Helix Transition Promoting Segments R. Rai, S. Raghothama, R. Sridharan, P. Balaram. Biopolymers (Peptide Science), 88, 350-361, 2007,

51 Tyrosine-heme ligation in Heme-peptide complex: design based on conserved motif of catalase Jagdish Rai, S. Raghothama, D. Sahal. Journal of Peptide Science. 13, 406-412, 2007.

52 De novo design of F containing heme binding peptides.Jagdish Rai, S. Raghothama, D. Sahal

Chemical Biology and Drug Design. 9, 119-123, 2007

53 Identification and characterization of a library of microheterogeneous cyclohexadepsipeptides from the fungus Isaria V. Sabareesh , R.S. Ranganayaki, S. Raghothama, M.P. Bopanna, Hema Balaram, M.C. Srinivasan and P. Balaram. J. Natural Products , 70, 715-729, 2007.

54. Isolation, Purification and Characterization of an Antifungal Molecule Produced by Bacillus licheniformis BC98, and its effect on phytopathogen Magnaporthe grisea. S.R. Tendulkar, Y.K. Saikumari, V. Patel, S. Raghotama, T.K.Munshi, P. Balaram . B.B. Chattoo, Journal of Applied Microbiology. 103, 2331-2339, 2007.

55. Hybrid Peptides: Expanding the Turn in Peptide Hairpins by the Insertion of and Residues Rai. R, Vasudev. P.G, Ananda, K, Raghothama. S, Shamala. N, Karle, I.L, and Balaram. P. Chem. Eur. J. 13, 5917-5926, 2007.

56. Designed peptides with homochiral and heterochiral diproline templates as conformational constraints. B. Chatterjee, I.Saha, S. Raghothama, S. Aravinda, R Rai, N. Shamala, P.Balaram. Chem. Eur. J. 14, 6192-6284, 2008.

57. Multiple Conformational States in Crystals and in Solution in αγ Hybrid Peptides. Fragility of the C12 Helix in Short Sequences. Sunanda Chatterjee, Prema G. Vasudev, Kuppanna Ananda, Srinivasarao Raghothama, Narayanaswamy Shamala, and Padmanabhan Balaram J. Org. Chem. 73, 6595-6606, 2008

58. Solid State and Solution Conformations of a Hybrid Hexapeptide. Characterization of a Backbone Expanded Analog of the -Polypeptide 310- Helix. Sunanada Chatterjee, Prema G. Vasudev, Srinivasarao Raghothama, Narayanaswamy Shamala, Padmanabhan Balaram. Biopolymers (Pept.Sci.), 90, 759-771, 2008.

59. Synthesis of 2-deoxy cyclic and linear oligosaccharides by oligomerization of monomers Somak Paul, Srinivasarao Raghothama, Narayanaswamy Jayaraman. Carbohydrate Research, 344, 177–186, 2009.

60. Expanding the Peptide -Turn in Hybrid Sequences: 12 Atom Hydrogen Bonded Helical and Hairpin Turns. S. Chatterjee, P. G. Vasudev, S. Raghothama, C. Ramakrishnan, N. Shamala, and P. Balaram. J. Am. Chem. Soc. 131, 5956-5965, 2009.

61. Natural Abundant Solid State NMR Studies in Designed Tripeptides for Differentiation of Multiple Conformers. S. Jayanthi, Bhaswati Chatterjee, S. Raghothama Biopolymers, 91, 851-860, 2009

62. Conformations of Heterochiral and Homochiral Proline- Pseudoproline Segments in Peptides. Context Dependent cis-trans Peptide Bond Isomerization

Kantharaju, S. Raghothama, U.S. Raghavender, S. Aravinda, N. Shamala, and P.Balaram. Biopolymers (Pept.Sci), 92, 405-416, 2009.

63. Ring Expansion of Oxyglycals. Synthesis and Conformational Analysis of Septanoside-Containing Trisaccharides. N.Vijaya Ganesh, S.Raghothama, R. Sonti, and N. Jayaraman. J. Org. Chem. 75, 215-218, 2010.

64. Helical conformations of hexapetpides containing N-terminal diproline segments. Kantharaju, S. Raghothama, S. Aravinda, N. Shamala, and P. Balaram. Biopolymers (Pept.Sci.), 94, 360-370, 2010.

65. Solution conformation of a tetradecapeptide stabilized by two di-n-propyl glycine residues. Vijayalekshmi Sarojini, R. Balaji Rao, S. Raghothama, and P.Balaram.

Journal of peptide Science, 16, 430-436, 2010.

66. Chemistry in confined spaces: High-energy conformer of a piperidine derivative is favored within a water-soluble capsuleplex. Mintu Porel, Nithyanandhan Jayaraj, S. Raghothama, and V. Ramamurthy. Org. Lett., 12, 4544–4547, 2010.

67. NMR of Peptides. S. Raghothama,

Journal of the Indian Institute of Science, 90, 145-161, 2010.

68. Effect of ester chemical structure and peptide bond conformation in fragmentation pathways of differently metal cationized cyclodepsipeptides.R. Banerjee, S. Sudarslal, R.S. Ranganayaki, and S. Raghothama

Org. Biomol. Chem., 9, 6234-6245, 2011.

69. NMR structure implications of enhanced efficacy of Obestatin fragment analogs. B. Krishnarjuna, A. D. Ganjiwale, U.V. Manjappara, S. Raghothama. Int. J. Pept. Res. Ther. 17, 259-270, 2011.

70. Chain length effects on helix-hairpin distribution in short peptides with Aib-DAla and Aib-Aib segments. A. Rajagopal, S. Aravinda, S. Raghothama, N. Shamala, P. Balaram.Peptide Science, 96, 744-756, 2011.

71. Aromatic interactions in model peptide -hairpins: Ring current effects on proton

chemical shifts.A. Rajagopal, S. Aravinda, S. Raghothama, N. Shamala, P. Balaram.Peptide Science, 98, 185-194, 2012.

72. Three-component self-assembly of a series of triply interlocked Pd12 coordination prisms and their non-interlocked Pd6 analogues.A.K. Bar, S. Raghothama, D.Moon, and P.S. Mujkherjee.Chem. Eur. J. 18, 3199-3209, 2012.

73. Helix and hairpin nucleation in short peptides using centrally positioned conformationally constrained dipeptide segments.S. Chandrappa, S. Aravinda, S. Raghothama. R. Sonti, R. Rai, V.V. Harini, N.Shamala, and P. Balaram.

Org. Biomol. Chem. 10, 2815-2823, 2012.

74. β-Turn Analogues in Model αβ-Hybrid Peptides: Structural Characterization of Peptides Containing β2,2Ac6c and β3,3Ac6c Residues.K. Basuroy, A. Rajagopal, S. Raghothama, N. Shamala , P. Balaram.Chem. Asian J, 7, 1671-1678, 2012.

75. Theoretical and in vitro studies of a C-terminal peptide from PGKC of Leishmania mexicana Mexicana. S. Kaushik, B. Krishnarjuna, S. Raghothama, S. Aggarwal, V. Raghunathan, A. Ganjiwale.

Mol Biochem Parasitol, 185, 27. 2012.

76. NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded -sheet peptide.

R. Sonti, R. Rai, S. Raghothama, P. BalaramJ. Phys. Chem. B 116, 14207-14215, 2012

77. Does Aluminium bind to Histidine? An NMR investigation in Aβ12 and Aβ16 fragments.Priya Narayan, B. Krishnarjuna2, V. Vinaya, D.Jagadeesh Kumar, K.V. Ramanathan, K.R.K Eswaran, H.G. Nagendra, S. Raghothama.

Chem. Bio. Drug. Des . 82, 48-59, 2013,

78. A Designed Three-Stranded -Sheet in an Hybrid Peptide. Rajesh Sonti, Hosahudya N. Gopi, Umashankara Muddegowda, Srinivasarao Ragothama, and Padmanabhan Balaram. Chem. Eur. J., 19, 5955-5965, 2013.

79. Stabilizing effect of electrostatic vs. aromatic interactions in diproline nucleated peptide -hairpins.

Kamlesh Madhusudan Makwana,a Srinivasarao Raghothama* and Radhakrishnan Mahalakshmi* Phys. Chem. Chem. Phys., 15, 15321-15324, 2013.

80. Unconstrained Homooligomeric γ-Peptides Show High Propensity for C14 Helix Formation

Krishnayan Basuroy, Bhimareddy Dinesh, M. B. Madhusudana Reddy, Siddapa Chandrappa,‡ Srinivasarao Raghothama,§ Narayanaswamy Shamala, and Padmanabhan Balaram. Org. Lett. 15, 4866-4869, 2013.

81. Conformational Diversity in Contryphans from Conus Venom: cis–trans Isomerisation and Aromatic/Proline Interactions in the 23-Membered Ring of a 7-Residue Peptide Disulfide Loop Rajesh. S, K. H.Gowd, K. N. Shashanka Rao, S. Ragothama, A.Rodriguez, J.J. Perez, and P.Balaram. Chem. Eur. J. 19, 15175-15189, 2013.

82. C12-Helix Development in (αγ)n Sequences – Spectroscopic Characterization of Boc–[Aib–γ4(R)Val]–OMe Oligomers B. Dinesh, V.Vinaya, S. Raghothama, and P. Balaram. Eur. J. Org. Chem., 3590–3596, 2013.

83. C12 Helices in Long Hybrid (αγ)n Peptides Composed Entirely of Unconstrained Residues with Proteinogenic Side Chains R. Sonti B. Dinesh, K. Basuroy, S. Raghothama, N. Shamala, and P. Balaram. Org. Lett. 16, 1656-1659, 2014.

84. Evaluation of hexane and ethyl acetate extracts of the sponge Jaspis diastra collected from Mauritius Waters on HeLa cells. G. Beedessee, A.Ramanjooloo, I. Tiscornia, S.Rao, D. Arya, K.H.Gowd, S. Raghotham, P.Balara, M. B-Fogolin, D. E.P Marie. Journal of Pharmacy and Pharmacology. (in press), 2014.

85. Conformational Analysis of a 20-Membered Cyclic Peptide Disulfide from Conus Virgo with a WPW Segment: Evidence for an Aromatic–Proline Sandwich. R. Sonti, K. N. Shashanka Rao, S. Chidanand, K. Hanumae Gowd, S. Raghothama, and P. Balaram. Chem. Eur. J, 20, 5075-5086, 2014.

86. Directing peptide conformation with centrally positioned pre-organized dipeptide segments: studies of a 12-residue helix and β-hairpin. S. Chandrappa, M.B. Madhusudana Reddy, R. Sonti, K. Basuroy. S. Raghothama, P.Balaram. Amino Acid. 47, 291-301, 2015.

87. Antimicrobial peptides with potential for biofilm eradication: Synthesis and structure

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88. Effects of hydrogen bonding on amide-proton chemical shiftanisotropy in a proline- containing model peptide. K. Pichumani, G. George, S. Hebbar, B. Chatterjee, S. Raghothama. Chem. Phys. Letts. 627, 126-129, 2015.

89. Effect of methylene group insertions on the structural rigidity of Aib containing helices A. Duley , V.Gowda, A. Ganjiwale , S. Raghothama* and G. Ramanathan* Peptide Science. 104, 720-732, 2015.

90. Exploring Structural Features of Folded Peptide Architectures in the Construction of Nanomaterials R. Misra, R. M. Reja, L.V. Narendra, G. George, S. Raghothama and H. N. Gopi. Chem. Commun., 52, 9597- 9600, 2016.