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Molecular Biophysics Unit, Indian Institute of Science, E-mail: pb{at}mbu.liisc.ernet.in
Anil Kumar Lala, Professor of Chemistry at the Indian Institute of Technology (IIT) Bombay and a member of the Editorial Board of Protein Science, died on July 17, 2004, following a stroke that he suffered three weeks earlier. Born on January 13, 1950, Lala received his B.Sc. from Delhi University and obtained his Ph.D. at Bombay University in 1974, working under the supervision of A.B. Kulkarni. His doctoral work was in the area of steroid chemistry, introducing him to the areas of NMR spectroscopy and mass spectrometry. Following a year at the Central Drug Research Institute in Lucknow, Lala moved to the State University of Ghent, Belgium, to work with Marc Anteunis. I first saw his name in a scientific publication when the conformational analysis of methionine enkephalin, then recently discovered as the endogeneous ligand for the opioid receptor, was described by the French and Belgian groups with Lala as a co-author (Roques et al. 1976). In 1976, he moved to Harvard University to work with Konrad Bloch. This period sparked his lifelong interest in membranes, specifically lipid-protein interactions. Lala joined the chemistry department at IIT, Mumbai, in 1979, where he spent the remaining 25 years of his scientific career.
By the 1970s, chemistry in India had a long tradition; organic chemistry was a bastion of synthetic and natural products chemistry. Biochemistry, too, was a well established discipline with a strong base in classical enzymology. Lala was among the first of a new generation of converts from chemistry who turned to problems of biological interest, labeling himself as a bioorganic chemist. New religions do not take root easily; Lala’s early years at IIT saw him struggle with great tenacity to establish work at the borders of chemistry and biology as an integral part of activity in a major chemistry department in India. Today, the term "chemical biology" is both fashionable and respectable in our academic institutions, a recognition that chemistry is indeed the "engine that drives biology." Anil Lala contributed in no small measure to this transformation in India, influencing a large number of students trained in traditional chemistry to seek the greener pastures of biology.
Lala’s early work at Bombay (now Mumbai) built upon his interests acquired at Harvard, studying the effect of modified cholesterol derivatives on yeast sterol auxotrophs and probing sterol-phospholipid interactions (Nanda Kumari et al. 1982; Ranadive and Lala 1987). But he also began to develop a new area, photolabeling, in which he was to make major contributions in the years to come. I believe his interest in this area may have been influenced by his years in Cambridge, Massachusetts, where he undoubtedly became aware of Frank Westheimer’s work at Harvard on nitrene photolabeling agents (Chowdhry and Westheimer 1979) and Har Gobind Khorana’s work at MIT on intermolecular crosslinking of acyl chains in phospholipids using a photoactivable carbene precursor (Gupta et al. 1979). Lala was quick to recognize the opportunity to develop highly reactive carbenes, capable of rapid insertion into neighboring chemical bonds upon generation by photolysis. His work on diazafluorene as a "new fluorescent photochemical reagent" provided an alternative to light activatable radio-labels (Anjaneyulu and Lala 1982). Over the last 20 years, Lala and an extraordinarily dedicated band of graduate students developed photolabeling into an important and powerful tool for analyzing the organization of proteins in membranes using the human erythrocyte glucose transporter, Staphylococcus aureus 
-toxin and diphtheria toxin as examples, where the utility of this method was clearly demonstrated (Lala et al. 1990; D’Silva and Lala 1998 D’Silva and Lala 2000). Lala sensed opportunities to exploit the techniques he developed for the characterization of protein folding intermediates (D’Silva and Lala 1999) and depth probing in phospholipids bilayers (Lala 2002). He had begun moving into a new area, the systematic characterization of scorpion neurotoxins over the last few years (Dhawan et al. 2003).
Anil Lala was an excellent organizer and the main architect of the Biosciences and Engineering program at IIT, which has now grown into a full fledged activity in biological sciences and biotechnology. He worked very hard to establish protein sequencing facilities, under difficult circumstances, and most recently set up a mass spectrometry facility to aid the cause of protein chemistry in Mumbai. He single-handedly championed the idea of setting up an Indian Protein Society, managing to recruit Bill DeGrado and other colleagues in the United States for the task of organizing a symposium in Mumbai partially sponsored by the Protein Society. The meeting held at IIT in October 2002 was a great success, bringing together an international gathering of protein chemists and structural biologists, a tribute to Anil Lala’s enthusiasm and powers of persuasion.
Anil Lala was an enthusiastic teacher, his words and ideas sometimes flowing too fast for the slow listener. But in teaching it is the passion for the discipline that makes the greatest impact on a beginning student. Anil possessed this passion in full measure, successfully inspiring many students to enter research careers. The IITs enjoy a high academic reputation in the world; many of their best students eventually turning to management, marketing and finance, drawn by the irresistible lure of business schools. The IITs have often advanced undergraduate engineering programs as the true measure of their "brand equity." But faculty like Anil Lala, who have on occasion drawn away bright engineering students to academic research, must be highly valued and celebrated.
Anil was a warm and generous friend and an enthusiast for science. I believe his best years were yet to come. He will be greatly missed by his family—wife, Krishna, and son, Vishal, and a host of friends and colleagues.
Footnotes
1 Based on an obituary that appeared in Current Science (87: 396.) 
References
Anjaneyulu, P.S.R., and Lala, A.K. 1982. Diazofluorene—a new reagent for fluorescent photochemical labelling of membrane hydrophobic core. FEBS Lett. 146: 165–167.[CrossRef]
Chowdhry, V. and Westheimer, F.H. 1979. Photoaffinity labeling of biological systems. Annu. Rev. Biochem. 48: 293–325.[CrossRef][Medline]
Dhawan, R., Varshney, A., Mathew, M.K., and Lala, A.K. 2003. BTK-2, a new inhibitor of the Kv1.1 potassium channel purified from Indian scorpion Buthus tamulus. FEBS Lett. 539: 7–13.[CrossRef][Medline]
D’Silva, P.R. and Lala, A.K. 1998. Unfolding of diphtheria toxin. Identification of hydrophobic sites exposed on lowering of pH by photolabeling. J. Biol. Chem. 273: 16216–16222.
———. 1999. Hydrophobic photolabeling as a new method for structural characterization of molten globule and related protein folding intermediates. Protein Sci. 8: 1099–1103.[Abstract]
———. 2000. Organization of diphtheria toxin in membranes. A hydrophobic photolabeling study. J. Biol. Chem. 275: 11771–11777. (Erratum in J. Biol. Chem. 2000. 275: 27500.)
Gupta, C.M., Radhakrishnan, R., Gerber, G.E., Olsen, W.L., Quay, S.C., and Khorana, H.G. 1979. Intermolecular crosslinking of fatty acyl chains in phospholipids: Use of photoactivable carbene precursors. Proc. Natl. Acad. Sci. 76: 2595–2599.
Lala, A.K. 2002. Fluorescent and photoactivable probes in depth-dependent analysis of membranes. Chem. Phys. Lipids 116: 177–188.[CrossRef][Medline]
Lala, A.K., Batliwala, H.F., and Bhat, S. 1990. Topography of multiple spanning transmembrane proteins—a photochemical approach. Pure Appl. Chem. 62: 1453–1456.
Nanda Kumari, S., Ranadive, G.N., and Lala, A.K. 1982. Growth of a yeast mutant on a ring A modified cholesterol derivative. Biochem. Biophys. Acta. 692: 441–446.[CrossRef]
Ranadive, G.N. and Lala, A.K. 1987. Sterol-phospholipid interaction in model membranes: role of C5–C6 double bond in cholesterol. Biochemistry 26: 2426–2431.[CrossRef][Medline]
Roques, B.P., Garbay-Jaureguiberry, C., Oberlin, R., Anteunis, M., and Lala, A.K. 1976. Conformation of Met5-enkephalin determined by high field PMR spectroscopy. Nature 262: 778–779.[CrossRef][Medline]
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