1. Cawthern, K. A., Narayan, M., Chaudhuri, D., Permyakov, E. A., Berliner, L. J. (1997) Interactions of  a-lactalbumin with fatty acids and spin label analogs. J. Biol. Chem. 272: 30812 30816.

  2. Narayan, M., Berliner, L. J. (1997) Fatty acids and retinoids bind independently and simultaneously to b‑lactoglobulin. Biochemistry 36: 1906 ‑1911.

  3. Narayan M., Wright, V. P., Berliner, L. J., Diaz, P. T., Merola A. J., Clanton, T. L. (1997) Do nitric oxide and peroxynitrite contribute to hydroxylation reactions in fatigued diaphragm? FASEB Journal 11: 72 72.       

  4. Narayan, M., Berliner, Merola, A. J., Diaz, P. T., Clanton, T. L. (1997) Biological reactions of peroxynitrite: evidence for an alternative pathway of salicylate hydroxylation Free Radical Research 27: 63 72.

  5. Narayan, M., Berliner, L. J. (1998) Mapping fatty acid binding to b‑lactoglobulin: ligand binding is restricted by modification of Cys 121 Protein Science 7: 150‑157.

  6. Veprintsev, D. B., Narayan, M., Permyakov, S. E., Uversky, V. N., Brooks, C. L., Berliner, L. J. (1999) Fine tuning the n-terminus of a calcium binding protein: -lactalbumin. Proteins 37: 65 72.

  7. Welker, E., Narayan, M., Volles, M. J., Scheraga, H. A. (1999) Two new structured intermediates in the oxidative folding pathway of Ribonuclease A. FEBS Letters 460: 477-479.

  8. Low, L. K., Shin, H.-C., Narayan, M., Wedemeyer, W. J., Scheraga, H. A. (2000) Accelerated refolding of bovine pancreatic ribonuclease A by phosphate induced stabilization of native-like intermediates. FEBS LETT. 472: 67-72.

  9. Narayan, M., Welker, E., Wedemeyer, W. J., Scheraga, H. A. (2000) Oxidative folding of proteins. Accounts of Chemical Research 11: 805-812. Invited Review Article

  10. Wedemeyer, W.J., Welker, E., Narayan, M., Scheraga, H.A. (2000) Disulfide bonds and protein folding. Biochemistry 39: 4207-4216. Invited Review Article

  11. Narayan M., Welker, E., Scheraga, H. A. (2001) Development of a novel method to study the rate-determining step during protein regeneration: Application to the oxidative folding of RNa47se A at low temperature reveals BPTI-like kinetic traps. J. Am. Chem. Soc. 123: 2909-2910.

  12. Welker, E. *Narayan, M., Wedemeyer, W. J., Scheraga, H. A. (2001) Dissecting the oxidative folding pathways of Ribonuclease A. Proc. Natl. Acad. Sci. USA 98: 2312-2316. (*equal contribution)

  13. Welker, E., Wedemeyer, W. J., Narayan, M., Scheraga, H. A. (2001) Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins Biochemistry 40: 9059-9064. Invited Review Article

  14. English, B. P., Welker, E., Narayan, M., Scheraga, H. A. (2002) Development of a novel method to populate native-disulfide-bonded intermediates for structural characterization of proteins: Implications for the mechanism of oxidative folding of RNase A. J. Am. Chem. Soc. 124: 4995-4999.

  15. Narayan M., Xu, G., Schultz, S. K., Scheraga, H. A. (2003) Assessing the Magnitude of Folding Forces along the Oxidative Folding Pathway of Multi-Disulfide-Containing Proteins. J. Am. Chem. Soc. 125: 16184-16185.

  16. Narayan, M., Welker, E., Scheraga, H. A. (2003) Characterizing the unstructured intermediates in oxidative folding. Biochemistry 42: 6947-6955.

  17. Narayan, M., Welker, E., Scheraga, H. A. (2003) Native conformational tendencies in unfolded polypeptides: Development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins. Journal of the American Chemical Society 125: 2036-2037.

  18. Narayan, M., Welker, E., Wanjalla, C., Xu, G., Scheraga, H. A. (2003) Shifting the competition between the intra-molecular reshuffling reaction and the direct oxidation reaction during the oxidative folding of kinetically-trapped disulfide-insecure intermediates. Biochemistry 42: 10783-10789

  19. Shin, H-S., Narayan, M., Song, M-C., Scheraga, H. A. (2003) Role of the [65-72] disulfide bond in oxidative folding of bovine pancreatic ribonuclease A. Biochemistry 42: 11514-11519.

  20. Welker, E., Narayan, M, Scheraga, H. A. (2003) Disulfide bonds in proteins. Encyc. Ref. of Genomics and Proteomics in Molecular Medicine. (Ganten, D. and Ruckpaul, K, Eds) Springer Verlag.

  21. Xu, G., Narayan, M., Welker, E., Scheraga, H. A. (2003) A novel method to determine thermal transition curves of disulfide-containing proteins and their structured folding intermediates. Biochemical and Biophysical Research Communications 311: 514-517.

  22. Chaudhuri, D., Narayan, M., Berliner, L. J. (2004) Conformation dependent interaction of α-Lactalbumin with model and biological membranes: A spin label ESR study. The Protein Journal 23: 95-101.

  23. Gahl, R. F., Narayan, M., Xu, G. and Scheraga, H. A. (2004) Trimethylamine-N-oxide modulates the reductive unfolding of onconase. Biochemical and Biophysical Research Communications 325: 707-710

  24. Narayan, M., Xu, G., Ripoll, D. R., Zhai, H., Breuker, K., Wanjalla, C., Leung, H. J., Navon, A., Welker, E., McLafferty, F. W., Scheraga, H. A. (2004) Dissimilarity in the reductive unfolding pathways of two Ribonuclease homologues. Journal of Molecular Biology 338: 795-809.

  25. Xu, G., Narayan, M., Welker, E., Scheraga, H. A. (2004) Characterization of the fast-forming intermediate, Des [30-75], in the reductive unfolding of Onconase  Biochemistry 43: 3246-54.

  26. Xu, G., Zhai, H., Narayan, M., McLafferty, F. W., Scheraga, H. A. (2004) Influence of oligosaccharides on the reductive unfolding of RNase B: Characterization by top down mass spectrometry of the unfolding pathways of a protein isoform mixture. Chemistry and Biology 11: 517-524.

  27. Leung, H. J., Xu, G., Narayan, M., Scheraga, H. A. (2005) Impact of an easily reducible disulfide bond on the oxidative folding rate of multi-disulfide-containing proteins. Journal of Peptide Research 65: 47-54.

  28. Xu, G., Narayan, M., Scheraga, H. A. (2005) The oxidative folding rate of bovine pancreatic ribonuclease is enhanced by a covalently attached oligosaccharide. Biochemistry 44: 9817-9823.

  29. Scheraga, H. A., Xu, G., Narayan, M., Pradeep, L (2006) Effect of Local Structure on the Reductive Unfolding Pathways of Ribonuclease A. The FASEB Journal 20: A501

  30. Xu, G., Narayan, M., Kurinov, I., Ripoll, D. R., Welker, E., Khalili, M., Ealick, S. E., Scheraga, H. A. (2006) A localized specific interaction alters the unfolding pathways of structural homologues. JACS 128: 1204-1213.

  31. Gomez, G., Mansouraty, G., Gardea, J., Narayan, M. (2007) Acceleration of oxidative protein folding by curcumin through novel non-redox chemistry. Biochemical and Biophysical Research Communications 364: 561-6.

  32. Welker, E., Hathaway, L., Xu, G., Narayan, M., Pradeep, L., Shin, H. C., Scheraga H. A. (2007) Oxidative folding and N-terminal cyclization of onconase. Biochemistry 46: 5485-93.

  33. Fink, M., Nieves, P., Chang, S., Narayan, M. (2008) Non-redox-active small-molecules can accelerate oxidative protein folding by novel mechanisms. Biophys. Chem. 132: 104-9.

  34. Gahl, R. F., Narayan, M., Xu, G., Scheraga, H. A. (2008) Dissimilarity in the oxidative folding of onconase and ribonuclease A, two structural homologues. Protein Eng Des Sel. 21: 223-31.

  35. Narayan, M., Welker, E., Zhai, H, Han, X, Xu, G, McLafferty, F. W., Scheraga, H. A. (2008) Detecting native-folds in mixtures of disulfide-bond-containing proteins. Nature Biotechnology 26: 427-9.

  36. Wang, Y. H., Narayan, M. (2008) pH dependence of the isomerase activity of protein disulfide isomerase: Insights into its functional relevance. Protein Journal  27: 181-5.

  37. Peralta-Videa, J. R., Lopez, M. L., Narayan, M., Saupe, G., Gardea-Torresdey, J. L. (2009) The biochemistry of environmental heavy metal uptake by plants: Implications for the food chain. International Journal of Biochemistry and Cell Biology 41: 665-77.

  38. Gonzalez, V.; Pal, R., Narayan, M. (2010) The oxidoreductase behavior of protein disulfide isomerase impedes fold maturation of ER-processed proteins in the pivotal structure-coupled step of oxidative folding: Implications for subcellular protein trafficking.  Biochemistry 49: 6282-6289.

  39. Pal, R., Gonzalez, V., Narayan, M. (2010) Reshuffling activity of protein disulfide isomerase reduces refolding yield in the structure-forming step of the oxidative protein folding reaction. Chemistry Letters 39: 263-265.

  40. Pal, R., Cristan, E. A., Schnittker, K., Narayan, M. (2010) Rescue of ER oxidoreductase function through polyphenolic phytochemical intervention: Implications for subcellular traffic and neurodegenerative disorders BBRC 392, 567-71.

  41. Pinales, L. A., Chianelli, R. R., Durrer, W. G., Pal, R., Narayan, M. Manciu, F. S. (2010) Spectroscopic study of inhibition of calcium oxalate calculi growth by Larrea tridentata. Journal of Raman Spectroscopy 42:259-264.

  42. Gardea, J., Rios, L., Pal, R., Gardea-Torresdey, J. L., Narayan, M. (2011) From folklore to molecular pharmacophores: Cultivating STEMs in young first-generation female Mexican-American Journal. of Chemical Education. 88: 41-43.

  43. Mahesh Narayan (2011) The Case of Oxidative Folding of Ribonuclease A: Factors impacting fold maturation of ER-processed proteins” Book Series-Protein Reviews (M. Zouhair Atassi); Book Name: Folding of disulfide proteins (Rowen JY Chang and Salvadore Ventura) Springer (

  44. Pal, R., Miranda, M., Narayan, M. (2011) Nitrosative stress-induced Parkinsonian Lewy-like aggregates prevented through polyphenolic phytochemical analog intervention.  Biochemical and Biophysical Research Communications 404: 324-9.

  45. Kabiraj, P., Pal, R., Varela-Ramirez, A., Miranda, M., Narayan, M. (2012) Nitrosative stress mediated misfolded protein aggregation mitigated by Na-D-β-hydroxybutyrate intervention. Biochemical and Biophysical Research Communications 426: 438-44.

  46. Narayan M. (2012) Disulfide bonds: protein folding and subcellular protein trafficking. FEBS Journal 279: 2272-82.

  47. Sirimulla, S., Pal, R., Raparla, M., Bailey, J. B., Duran, R., Altamirano, A. M., Herndon, W. C., Narayan, M. (2012) Identification of novel nitrosative stress inhibitors through virtual screening and experimental evaluation (2012) Molecular Informatics 31: 167-172.

  48. 48.Sirimulla, S., Bailey, J. B., Vegesna, R., Narayan, M. (2013) Halogen interactions in protein-ligand complexes: implications of halogen bonding for rational drug design. Journal of Chemical Information and Modeling 53: 2781-91.

  49. Arumugam A, Agullo P, Boopalan T, Nandy S, Lopez R, Gutierrez C, Narayan M, Rajkumar L. (2014) Neem leaf extract inhibits mammary carcinogenesis by altering cell proliferation, apoptosis, and angiogenesis. Cancer Biol Ther. 15: 26-34. (Cover)

  50. Kabiraj, P., Marin, J. E., Varela-Ramirez, A., Zubia, E., Narayan, M. (2014) Ellagic acid mitigates SNO-PDI induced aggregation of Parkinsonian biomarkers. ACS Chemical Neuroscience 5: 1209-20.

  51. Kabiraj, P., Marin, J. E., Varela-Ramirez, A., Zubia, E., Narayan, M. (2014) Ellagic acid mitigates SNO-PDI induced aggregation of Parkinsonian biomarkers. ACS Chemical Neuroscience 5: 1209-20.

  52. A. Khalil, M. F., Valenzuela, C., Sisniega, D., Skouta, R., Narayan, M. (2015) ER Protein Processing under oxidative stress: Implications and Prevention (2016) Cell Biochemistry and Biophysics International 74: 213-20.

  53. B. Subramani, R., Gonzalez, E., Arumugam, A., Nandy, S., Gonzalez, V., Medel, J., Camacho, F., Ortega, A., Bonkoungou, S., Narayan, M., Dwivedi, A. K., Lakshmanaswamy, R. (2016) Nimbolide inhibits pancreatic cancer growth and metastasis through ROS-mediated apoptosis and inhibition of epithelial-to-mesenchymal transition. Nature Scientific Reports 6:19819. doi: 10.1038/srep19819.

  54. Kabiraj, P., Marin, J. E., Varela-Ramirez, A., Narayan, M. (2016) : "A 11-mer amyloid beta peptide fragment provokes chemical mutations and Parkinsonian biomarker aggregation in dopaminergic cells: a novel roadmap for “transfected” Parkinson’s" ACS Chemical Neuroscience 7:1519-1530

  55. Koebel MR, Cooper A, Schmadeke G, Jeon S, Narayan M, Sirimulla S. (2016) S···O and S···N Sulfur Bonding Interactions in Protein-Ligand Complexes: Empirical    Considerations and Scoring Function. J Chem Inf Model.;56 :2298-2309.

  56. Kerstiens, C. G., Gunn, B. M. Becvar, J. E., Narayan, M. (2017) Untangling Chemical Kinetics through Tangible and Visual Representation of Matter African Journal of Chemical Education 7:37-45

  57. Mendez L, Henriquez G, Sirimulla S, Narayan M. Molecules. (2017) Looking Back, Looking Forward at Halogen Bonding in Drug Discovery. 22 pii: E1397. doi: 10.3390/molecules22091397. Review.

  58. Tasnim, N., Nair, B. G., Sai Krishna, K., Kalagara, S., Narayan, M., Noveron, J. C. &   Joddar, B. 2017 SpringerBriefs in Applied Sciences and Technology. 9789811032820 ed. Springer Verlag

  59. The Structure-Forming Juncture in Oxidative Protein Folding: What Happens in the ER?   Narayan, M. Adv Exp Med Biol. 2017 Aug 17. doi: 10.1007/5584_2017_88. [Epub ahead of print]

  60. Serrano M, Gonzalez V, Ray S, Chavez MD, Narayan M.Identification of Structure-Stabilizing Interactions in Enzymes: A Novel Mechanism to Impact Enzyme Activity Cell Biochem Biophys. 2017 Jul 29. doi: 10.1007/s12013-017-0816-3.

  61. Narayan, G. M. and Narayan, M. (2017) The thumb rule reveals: facilitating the transition from electron geometry to molecular geometry and vice versa African Journal of Chemical Education 7(3) 118-126.


  1. Mahesh Narayan Biochemistry Laboratory Manual, Kendal Hunt (ISBN:9781602501829)

  2. Gunn Mahmoud Narayan General Chemistry Lab Manual, Kendal Hunt (ISBN-10: 1602501998

  3. Gunn Mahmoud Narayan General Chemistry Lab Manual, Kendal Hunt ISBN-13: 9781602501997)

  4. Becvar, J. E., Noveron, J. C., Saupe, G.B., and Narayan, M. (2012-13) Hayden-McNeil, Plymouth MI

  5. Becvar, J.E., Narayan, M., Noveron, J.C., Saupe, G. B. (2012-13) Hayden-McNeil, Plymouth MI


Educational Workbooks Published by Lead for American Corporation (LFAC), a non-profit organization founded by James E. Becvar, Mahesh Narayan and Geoffrey B. Saupe, to promote Peer Lead Team Learning in schools and colleges world wide (   While the founding directors oversee every aspect of the workbook and educational design, since 2012 they have assumed the role of Publishers and invited Peer Leaders to contribute material to LFAC. The founding directors have delegated authorship rights to those peer Leaders and educators who create pedagogical material (for LFAC and its board who are the publishers).