(* senior author)


The Singapore times (> end 2003):



1.        *G G Dodson, D P Lane, C Verma, Molecular simulations of protein dynamics: new windows on mechanisms in biology EMBO Reports 9:144-150 (2008)

2.        *C J Brown, D Srinivasan, L H Jun, D Coomber, C S Verma, D P Lane The electrostatic surface of MDM2 modulates the specificity of its interaction with phosphorylated and unphosphorylated p53 peptides Cell Cycle (2008)

3.        A Dey, C S Verma, D P Lane. Update on p53: modulation of p53 degradation as a therapeutic apporoach. Invited review British J Cancer 98:4-8 (2008)

4.        S Gul, M P. Thomas, S Hussain, C S Verma, E W Thomas, K Brocklehurst Investigation of interactions within the active centre of papain using cationic reactivity probes designed to bind to Asp158 and react with the thiolate anion component of the (Cys25)–S–/(His159)–Im+H ion-pair Biochemistry  47:2025-2035  (2008)

5.        S Liu, L Zhou, J Li,  A. Suresh, C.S. Verma, Y H Foo, E.Yap, D. Tan  and R.W. Beuerman De Novo Linear Analogs of Human b-Defensin 3: Concept for Design of Antibacterial Peptides with Reduced Cytotoxicity to Mammalian Cells. ChemBioChem (2008)

6.        *A Madhumular, D J smith, C Verma. Stability of the core domain of p53: insights from computer simulations BMC Bioinformatics (2008) 9(Suppl 1):S17

7.       *Modulation of the p53-MDM2 interaction by phosphorylation of Thr18: a computational study H J Lee, D Srinivasan, D Coomber, D P Lane, C S Verma Cell Cycle 6:2604-11 (2007)

8.       *Defensins: Antimicrobial peptides for therapeutic development C Verma, S Seebah, L Soo Mei, Z Lei, L Shou Ping, L Jing, R Beuerman  Bitoechn J 2:1353-9 (2007)

9.       *Substrate specificity of Cyclins determined by electrostatics H J Lee, G H Chua, A Krishnan, D. P. Lane. C. S. Verma Cell Cycle 6:2219-26 (2007)

10.    *Wavelet analysis of protein dynamics K H Kiat, H J Lee, B Veeravalli, C Verma Lecture Notes in Bioinformatics (2007)

11.    *Enthalpic and entropic contributions in the transesterification of sucrose: computational study of lipases and subtilisin G. Fuentes, A. Ballesteros, C S Verma J Biomol Str Dyn 25:145-55 (2007)

12.    On the resolution of chiral substrates by a retro-Claisenase enzyme. Biotransformations of heteroannular bicylcic b-diketones by 6-oxo camphor hydrolase. C. L. Hill, C. H. Lee, D. J. Smith, C. S. Verma, G. Grogan Adv Synth Catal 349:1353-60 (2007)

13.    Desymmetrisations of 1-alkylbicyclo[3.3.0]octane-2,8-diones by enzymatic retro-Claisen reaction yield optically enriched 2,3-substituted cyclopentanones. C. L. Hill, C. S. Verma, Gideon Grogan Adv Synth Catal 349:916-24 (2007)

14.    *Hydration of hydrophobic moieties: A simulation study of interleukin-1beta. S Somani, C. P Chng, C. S. Verma. Proteins: Str Fn Gen 67:868 (2007)

15.    *Defensins Knowledgebase: A manually curated database and information source focused on the defensins family of antimicrobial peptides. S. Seebah, A. Suresh, R. Beuerman, C. S. Verma. Nucleic Acids Res 35: D265 (2007)

16.    *Oligomerization in defensins: a modelling study across mammals. A Suresh, C Verma BMC Bioinformatics 7:S17 (2006)

17.     *M. Ortiz-Lombardia, C S Verma Proteins as data storage devices: insights from computer models  J Phys: Conf Ser 34 7-14 (2006)

18.     W. G. Lim, B. J. Tan, Y Zhu, S. Zhou, J. S. Armstrong, Q. T. Li, Q. Dong, E. Chan, D. Smith, C. Verma,  S-L Tan & W. Duan The very C-terminus of PRK1/PRK is essential for its activation by RhoA and downstream signalling.   Cellular Signalling 18:1473-1481 (2006)

19.     Leonard PM, Brzozowski AM, Lebedev A, Marshall CM, Smith, DJ, Verma, CS, Walton, NJ and Grogan G The 1.8 Å resolution structure of hydroxycinnamoyl-coenzyme A hydratase-lyase (HCHL) from Pseudomonas fluorescens, an enzyme that catalyses the transformation of feruloyl-coenzyme A to vanillin  Acta Cryst. D62, 1494-1501 (2006)

20.     S. S. Yeong, Y. Zhu, D. Smith, C. Verma, W. G. Lim, B. J. Tan, J. A. Armstrong, S. Zhou, S-L Tan, N.S. Cheung & W. Duan The last ten amino acid residues beyond the hydrophobic motif are critical for the catalytic competence and function of protein kinase Ca.  J. Biol. Chem 281:30768-30781 (2006)

21.     M Witkowska-Zimny; M M Hryniewicz; P Neumann; A J. Wilkinson; A M. Brzozowski; C S. Verma; J Zaim; G D. Bujacz   Structural Basis of the Sulfate Starvation Response in E. coli: Crystal Structure and Mutational Analysis of the Cofactor-Binding Domain of the Cbl Transcriptional Regulator E Stec; J Mol Biol 364:309-322 (2006).

22.     *S. Vijayakrishnan, R. Qaamra, C. S. Verma, R. Sen & S. Mande Molecular Dynamics Simulations of the M. tuberculosis chaperonin-10: the role of metal ions  J Biomol Str Dyn 23:365-375 (2006)

23.     Y. Zhu, D. Smith, C. Verma,  W. G. Lim, B. J. Tan, J. S. Armstrong, S. Zhou, E. Chan, S-L Tan, Y-Z Zhu, N. S. Cheung & W. Duan The very C-terminus of protein kinase C is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependant kinase-1 Cellular Signalling 18:807-818 (2006)

24.     *G G Dodson & C S Verma. Protein flexibility: role in structure and mechanism revealed by molecular simulations Cell Mol Life Sci  63:207-219 (2006)

25.     C. S. Allardyce, P. J. Dyson, C. S. Verma, J. Coffey & N. Johnson. Characterisation of the transferrin cisplatin-binding site using mass spectrometry and molecular modelling. ChemBioChem  6 1788-1795 (2005)

26.     *M. Akif, K. Suhre, C. Verma, S.C. Mande Conformational flexibility of M. tuberculosis Thiredoxin reductase: crystal structure and normal mode analysis Acta Cryst Sect D   D61:1603-1611 (2005)

27.     *V. Renugopalakrishnan, M Ortiz-Lombardia, C Verma Electrostatics of cytochrome-c assemblies J Mol Model.11 :265-270 (2005)

28.     V Renugopalakrishnan, R Garduno-Juarez, G Narasimhan, C S Verma, X Wei and P Li Rational design of thermally stable proteins: relevance to bionanotechnology (Review). Jl Nanosci Nanotech 5 1759-1767 (2005)

29.     A. De Simone, G. G. Dodson, C. S. Verma, A. Zagari, F. Fratarnali. Prion dry spots and water hot spots: key roles for structural stability Proc Natl Acad Sci USA 102:7535-7540 (2005)

30.     K R Sakharkar, M K Sakharkar, C Verma, V T K Chow Comparative study of overlapping genes in bacteria, with special reference to Rickettsia prowazekii and Rickettsia conorii Int J Syst Evol Microbiol. 55 1205-9 (2005)

31.     *C S Verma & S Fischer Protein stability & ligand binding: new paradigms from in-silico experiments, Biophys Chem 115 295-302 (2005)

32.     A. Kumar, P. C. Mishra, M. Durai, C. S. Verma and V. Renugopalakrishnan A Density Functional Study of the Heme Moiety of Cytochrome c Int J Quant Chem 102 1002-1009 (2005)

33.     *G. L. Fuentes, A. R. Ballesteros & C. S. Verma Dynamic control of specificity in enzymes: computational study of transesterification of sucrose using lipases Protein Science 13 3092-3103  (2004)

34.     *R. B. Greaves, G. G. Dodson, C. S. Verma. Altered ionisation of the B13-Glu in insulin mutants: a computational analysis.  Protein Eng. Des. Sel. 17  557 – 563 (2004)

35.     H. J. Dubbink, R. Hersmus, M. van Royen, C. S. Verma­­­­, J. van Tol, A. C. J. Ziel-van der Made, A. O. Brinkmann, A. B. Houtsmuller, A. C.W. Pike, J. Trapman Distinct modes of recognition of FXXLF and LXXLL motifs by the androgen receptor Molecular Endocrinology 18 2132-2150 (2004).

36.     J. L. Whittingham, I. Jonassen, S. Havelund, S. M. Roberts, E. J. Dodson, C. S. Verma and G. G. Dodson. Crystallographic analysis and solution studies of N-lithocholyl insulin: a new generation of prolonged-acting insulins. Biochemistry 43 5987-5995 (2004)

37.     M. Prabhakaran, S. H. Gursahani, C. S. Verma, R. Garduno- Juarez, and V. Renugopalakrishnan. Cytochrome C: The effect of temperature and pressure from molecular dynamics simulations J. Phys. Chem. Solids 65 1615-1622 (2004)

38.     L. F. Haire, S. M. Whyte, N. Vashisht, A. C. Gill, C. Verma, E. J. Dodson, G. G. Dodson and P. M. Bayley. The crystal strucure of a truncated sheep prion protein J. Mol. Biol 336 1175-1183 (2004).




Pre-Singapore era (< end 2003 – The York times):


Chapters in Books:

·       K.Brocklehurst, A.B.Watts, M.Patel, C.Verma & E.W.Thomas Cysteine Proteinases: in Comprehensive Biological Catalysis: ed. M. Sinot, Academic Press, 1998.

·       R. Gill, C. Verma, J. Pitts, P. De-Meyts, A. Wollmer, S. Wood. Structure and function of human IGF-1: In Recent research developments in protein engineering, Vol 1, Research Signpost Publication, India (in press 2002).


1.        *N. P. Barton, C. S. Verma & L. S. D. Caves. Inherent flexibility of calmodulin domains: a normal mode analysis study: II J. Phys. Chem. B 107 2170-2170 (2003)

2.      S. Hussain, S. Pinitglang, T. S. F. Bailey, J. D. Reid, M. A. Noble, M. Resmini, E. W. Thomas, R. B. Greaves, C. S. Verma, K. Broklehurst.Variation in the pH-dependant pre-steady state and steady state kinetic characteristics of cysteine proteinase mechanism. Evidence for eletrostatically-modulation of ctaytic function by the neighbouring carboxylate  Biochem J 372 735–746 (2003)

3.        *Primary and 3-d modelled structures of two cyclotides from Viola odorata. Erika Svangårda, U.Göransson, D.Smith,C.Verma,A. Backlund, L. Bohlin, P. Claeson Phytochemistry 64 135-142 (2003)

4.        G. Grogan, J. L. Whittingham, J. P. Turkenberg, C. S. Verma, M. Walsh. The 2.0A resolution crystal structure of 6-oxo camphor hydrolase reveals unexpected structural diversity n the crotonase superfamily J. Biol. Chem. 278 1744-1750 (2003)

5.        *N. P. Barton, C. S. Verma, L. S. D. Caves Inherent Flexibility of Calmodulin Domains: A Normal-Mode Analysis Study    J. Phys. Chem. B. 106(42) 11036-11040 (2002)

6.        *G. Fuentes, M. A. Cruces, F. J. Plou, A. Ballesteros & C. S. Verma Computational studies of transesterification of sugars using subtilisins: importance of entropic effects ChemBioChem 3 907-910 (2002)

7.        A. A. McCarthy, M. A. Walsh, M. Reinhold, C. S. Verma, D. P. O’Connell, G. N. Yalloway, D. d’Arcy, T. M. Higgins, G. Voordouw, & S. G. Mayhew. Crystallographic investigation of the role of aspartate 95 in the modulation of the redox potentials of Desulfovibrio vulgaris flavodoxin Biochemistry 41 10950-10962 (2002)

8.        A. M. Brzozowski, F. De Beer, E. J. Dodson, G. G. Dodson, G. N. Murschudov, C. S. Verma, J. P. Turkenberg & Z. Dauter. Crystal structure of human insulin-like growth factor at 2.0A resolution: structural origins of hIGF-I and insulin functional divergence Biochemistry 41 9389-9397 (2002)

9.        S. Krzywda, A. M. Brzozowski, C. Verma, K. Karata, T. Ogura & A. J. Wilkinson. The crystal structure of the AAA domain of the ATP-dependant protease FtsH of Eschericia Coli at 1.5A resolution. Structure 10 1073-1083 (2002)

10.     *J. C. Smith, F. Merzel, C. S. Verma & S. Fischer. Protein hydration water: structure and thermodynamics J. Mol. Liq 101 27-33 (2002)

11.     *R. Dvorsky, J. Sevcik, V. Hornak, G.P.Tyrrell, L.S.D.Caves & C.S.Verma. Molecular dynamics simulations of Rnase-Sa: a window complementary to NMR/Xray J. Phys. Chem B 106 6038-6048 (2002)

12.     L.S.D.Caves & C.S.Verma Congruent behaviour of complete and reconstructed phase space trajectories from biomolecular dynamics simulation Proteins: Str Fn Gen 47 25-30 47 25-30 (2002)

13.     *S. Fischer, J. Smith & C. S. Verma Dissecting the vibrational entropy change on protein/ligand binding: burial of a water molecule in bovine pancreatic trypsin inhibitor J Phys Chem B  105 8050-8055 (2001)

14.     J. Reid, S. Hussain, S. Srredharan, T. Bailey, S. Pinitglang, E. Thomas, C. Verma & K. Brocklehurst. Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic obseravtion of dithioester intermediates, kinetic analysis and molecular dynamics simulations Biochem J 357 343-352 (2001)

15.     K. Karata, C. S. Verma, A. J. Wilkinson & T. Ogura. Probing the mechanism of ATP hydrolysis and substrate translocation in the AAA protease FtsH by mutagenesis and modeling Molecular Microbiology 39 890-903 (2001)

16.     Crystal structure of GerE, the ultimate transcriptional regulator of spore formation in Bacillus subtilis. V.M.A. Ducros, R..J. Lewis, C..S.Verma, E.J.Dodson, G.Leonard, J.P.Turkenberg, G.N.Murshudov, A.J.Wilkinson & J.A.Brannigan J. Mol. Biol. 306, 759-771 (2001)

17.     A. A. Antson, D. J. Smith, D. I. Roper, S. Lewis, L. S. D. Caves, C. S. Verma, S. L. Buckley, P. J. Lillford & R. E. Hubbard. The mechanism of ice binding by type III antifreeze proteins J. Mol. Biol. 305, 875-889 (2001)

18.     *R. Dvorsky, J. Sevcik, L.S.D. Caves & C. S. Verma.Temperature effects on protein motions: a molecular dynamics study of Rnase-Sa J Phys Chem B 104 10387-10397 (2000)

19.     A.M. Brzozowski, H. Savage, C. S. Verma, J. P. Turkenburg, D. M. Lawson, A. Svendsen & S. Patkar. Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase Biochemistry 39 15071-15082 (2000).

20.     L. Hewitt, V. Kasche, K. Lummer, R. J. Lewis, G. N. Murshudov, C. S. Verma, G. G. Dodson & K. Wilson. Structure of a slow processing precursor penicillin acylase from Escherichia Coli revelas the linker peptide blocking the active site cleft. J. Mol. Biol 302 887-898 (2000)

21.     M. A. Noble, S. Gul, C. S. Verma & K. Brocklehurst. The ionization characteristics and chemical influences of D158 of papain and caricain determined by structure-related kinetic and computational techniques: multiple electrostatic modulators of active centre chemistry. Biochemical Journal 351, 723-733 (2000).

22.     *S. Fischer & C. S. Verma. Binding of buried water increases the flexibility of proteins. Proc. Nat. Acad. Sci USA 96, 9613-9615 (1999).

23.     L. Tang, J. L. Whittingham, C. S. Verma, L. S. D. Caves & G. G. Dodson. Structural consequences of the B5 His->Tyr mutation in human insulin characterized by X-ray crystallography and conformational analysis. Biochemistry 38, 12041-12051 (1999).

24.     R. Gill, C. Verma, B. Wallach, , B. Urso, J. Pitts, A. Wollmer, P. Demeyts & S. Woods. Disulphide swapping in human insulin-like growth factor: implications for receptor binding. Protein Engg  12, 297-303 (1999))

25.     C. G. Suresh, A. V. Pundle, H. SivaRaman, K. N. Rao, J. A. Brannigan, C. McVey, C. S. Verma, Z. Dauter, E. J. Dodson,& G. G. Dodson. Penicillin V Acylase crystal structure reveals new Ntn-hydrolase family members. Nature Structural Biology 6, 414-416 (1999)

26.     *S. Jääskeläinen, C. S. Verma, L. S. D. Caves & R. E. Hubbard. Identifying key electrostatic interactions in Rhizomucor miehei lipase: the role of solvent dielectric. Theoretical Chemistry Accounts 101, 175-179 (1999).

27.     D. G. Truhlar, W. L. Jorgensen, M. T. Nguyen, J. B. Anderson, D. Chandler, S. HammesSchiffer, P. G. Bolhuis, I. H. Hillier, C. Dellago, J. N. L. Connor, M. V. Basilevsky, J. C. Tully, J. M. Bowman, E. M. Goldfield, G. Katz, T. J. Martinez, W. Jakubetz, H. W. Schranz, K. J. Schulten, M. Sprik, G. C. Schatz, J. T. Hynes, I. H. Williams, P. R. Taylor, C. S. Verma, A. Lagana, K. Morokuma, C. Trindle, H. F. Schaefer, N. A. Burton & L. Blancafort. General discussion Faraday  Disscn., 110, 477-520  (1999).

28.     J. H. Ullah, T. R. Walsh, I. A. Taylor, D. C. Emery, C. S. Verma, S. J. Gamblin & J. Spencer  The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7A resolution J. Mol. Biol. 284, 125-136 (1998).

29.     *S. Jääskeläinen, C. S. Verma, R. E. Hubbard, P. Linko & L. S. D. Caves. Probing the conformational change in the activation of lipase Protein Science, 7, 1359-1367 (1998).

30.     *S. Fischer, C. S. Verma & R. E. Hubbard. Rotation of buried water inside a protein: calculation of the rate and vibrational entropy of activation: J Phys Chem B, 102, 1797-1805  (1998).

31.     S. Pinitglang, A. B. Watts, M. Patel, J. D. Reid, M. A. Noble, S. Gul, A. Bokth, A. Naeem, H. Patel, E. W. Thomas, S. K. Sreedharan, C. Verma & K. Brocklehurst. A classical enzyme active centre motif lacks catalytic competence until modulated electrostatically. Biochemistry, 36, 9968-9982 (1997).

32.     M. Resmini, R. Vigna, C. Simms, N. J. Barber, E. P. Hagi-Pavli, A. B. Watts, C. Verma, G. Gallacher & K. Brocklehurst. Characterisation of the hydrolytic activity of a polyclonal catalytic antibody preparation by pH-dependence and chemical modification studies. Evidence for the involvement of Tyr and Arg sidechains as hydrogen bond donors. Biochemical Journal, 326, 279-287 (1997).

33.     *C. S. Verma, L. S. D. Caves, R. E. Hubbard & G. C. K. Roberts. Domain motions in dihydrofolate reductase: a molecular dynamics study. J Mol Biol, 266, 776-796 (1997).

34.     J. Plou, D. Kowlessur,  J. P. G. Malthouse, G. W. Mellor, M. J. Hartshorn, S. Pinitglang, H. Patel, C. M. Thomas, E. W. Thomas, C. Verma & K. Brocklehurst. Characterization of the electrostatic perturbation of a catalytic site (Cys)-S-/(His)-Im(+)H ion-pair in one type of serine proteinase architecture by kinetic and computational studies on chemically mutated subtilisin variants. J Mol Biol, 257, 1088-1111 (1996).

35.     R. Gill, B. Wallach, C. Verma, B. Urso, E. Dewolf, J. Grotzinger, J. MurrarRust, J. Pitts, A. Wollmer, P. Demeyts & S. Woods. Engineering the C-region of human Insulin-like Growth Factor-I - implications for receptor binding. Protein Engineering, 9, 1011-1019 (1996).

36.     K. Sreedharan, C. Verma, L. S. D. Caves, S. M. Brocklehurst, S. E. Gharbia, H. N. Shah & K.Brocklehurst. Demonstration that 1-trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane (E-64) is one of the most effective low (Mr) inhibitors of trypsin-catalyzed hydrolysis. Characterization by kinetic analysis and by energy minimization and moelcular dynamics simulation of the E64-b-trypsin complex.  Biochemical Journal, 316, 777-786 (1996).

37.     *C. S. Verma, S. Fischer, L. S. D. Caves, G. C. K. Roberts & R. E. Hubbard. Calculation of the reaction pathway for the aromatic ring flip in methotrexate complexed to dihydrofolate reductase. J Phys Chem, 100, 2510-2518 (1996).

38.     P. Thomas, C. Verma, S. M. Boyd & K. Brocklehurst. The structural origins of the unusual specificities observed in the isolation of chymopapain-M and actinidin by covalent chromatography and the lack of inhibition of chymopapain-M by cystatin. Biochemical Journal, 306, 39-46 (1995).

39.     M. Lawson, A. M. Brozozowski, S. Rety, C. Verma & G. G. Dodson. Probing the nature of substrate binding in Humicola Lanuginosa lipase through X-ray crsytallographic and intuitive modelling. Protein Engineering, 7, 543-550 (1994).

40.     C. S. Verma, M. Green & R. M. Wing. Kinetic recognition of the 5'-phosphate group in the attack of cisplatin type systems on DNA. Journal of the Chemical Society - Chemical Communications. 884-886 (1988).

41.     S. Gul, S. Pinitglang, E. W. Thomas, C. Verma & K. Brocklehurst. Senistivities of transition state geometries to P1-P2 binding in reactions of papain and actinidin. Biochemical Society Transactions 26, S171 (1998).

42.     A. Khan, I. F. Connerton, N. J. Cummins, S. Hussain, M. A. Noble, M. A. J. Taylor, E. W. Thomas, C. Verma & K. Brocklehurst. The kinetically influential ionizations of caricain D158N revealed by using 4,4’-dipyrimidyl disulfide as a reactivity probe. Biochemical Society Transactions 26, S172 (1998).

43.     K. Brocklehurst, E. W. Thomas, C. Verma, M. Patel & S. K. Sreedharan. Design and synthesis of substrate-derived N-acylaminoalkyl 2-pyridyl disulphides as probes of cysteine proteinase mechanism. Biochemical Society Transactions 25, 92S (1997).

44.     S. Gul, A. Clarke, B. Field, M. P. Thomas, F. Willenbrock, S. Pinitglang, C. Verma, E. W. Thomas & K. Brocklehurst. Investigation of the electrostatic field of the papain active centre by using monoprotonated and diprotonated pyridyl (pY) disulphides as reactivity probes. Biochemical Society Transactions 25, 91S (1997).

45.     M. Noble, D. Abramson, C. Verma & K. Brocklehurst. Evidence that the carboxy groups of Asp158 in papain and caricain have abnormally low pKa values and thus do not contribute the key ionisations with pKa 4 that generate catalytic competence. Biochemical Society Transactions 25, 90S (1997).

46.     B. Reid, S. Pinitglang, C. P. Thomas, C. Verma, E. W. Thomas & K. Brocklehurst. Actinidin and chymopapain B provide variation in the common electrostatic environment of Glu50 in papain and caricain. Biochemical Society Transactions, 25, 89S (1997).

47.     S. Pinitglang, M. Patel, M. Noble, S. K. Sreedharan, C. Verma, E. W. Thomas & K. Brocklehurst. Effects of the quality of the P2-S2 hydrophobic contacts on the catalytic activities of papain, caricain and ficin and their generation by electrostatic switches. Biochemical Society Transactions, 25, 88S (1997).

48.     A Watts, A. Hafeez, S. Gul, C. Verma & K. Brocklehurst. Effects of site-specific mutatons on the kinetically influential ionisations of papain. Biochemical Society Transactions, 25, 84S (1997).

49.     S. Gul, P. S. Dhillon, C. Verma, E. W. Thomas & K. Brocklehurst. Investigation of electrostatic interactions and binding effects in papain-ligand interaction. Biochemical Society Transactions 24, 473S (1996).

50.     S. Pinitglang, M. Noble, C. Verma, E. W.  Thomas & K. Brocklehurst. Studies on the enhancement of the reactivity of the Cys25-S-/His159-Im+H ion-pair of papain by deprotonation across pKa 4. Biochemical Society Transactions 24, 468S (1996).

51.     M. Green, S. S. Eapen, D. J. Evans, K. Percival, C. Verma & R. M. Wing. Rates of reaction of Guanosine derivatives with cis-[pt(NH3)2(OH2)2] & cis-[Pt(NH3)2(OH2)(OH)]. Recueil Des Travaux Chimiques des Pays-Bas 106, 194 (1987).


(* corr author)