Investigating the folding pathway and substrate induced conformational changes in B. malayi Guanylate kinase

International Journal of Biological Macromolecules

Volumn 94, Issue , 2017, Pages 621-633

  Gupta, Smita ^a   Yadav, Sunita ^a   Suryanarayanan, Venkatesan ^b   Singh, Sanjeev K ^b   Saxena, Jitendra K ^a  

^a CENTRAL DRUG RESEARCH INSTITUTE   (India)

^b ALAGAPPA UNIVERSITY   (India)

Author keywords

B. malayi Guanylate Kinase; Molten globule; Unfolding

Indexed keywords

ADENOSINE TRIPHOSPHATE; GUANIDINE; GUANOSINE PHOSPHATE; GUANYLATE KINASE; UREA; CROSS LINKING REAGENT; GLUTARALDEHYDE; HELMINTH PROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN;

ARTICLE; BRUGIA MALAYI; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STABILITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; MOLECULAR DOCKING; MOLECULAR DYNAMICS; NONHUMAN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN UNFOLDING; STRUCTURE ACTIVITY RELATION; SUBSTRATE CONCENTRATION; THERMOSTABILITY; ANIMAL; CHEMISTRY; ENZYMOLOGY; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; METABOLISM; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE;

ADENOSINE TRIPHOSPHATE; ANIMALS; BRUGIA MALAYI; CROSS-LINKING REAGENTS; ESCHERICHIA COLI; GENE EXPRESSION; GLUTARAL; GUANIDINE; GUANOSINE MONOPHOSPHATE; GUANYLATE KINASES; HELMINTH PROTEINS; MOLECULAR DOCKING SIMULATION; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; UREA;

EID: 84994056617     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2016.10.008     Document Type: Article

References (39)

1. [1] Ptitsyn, O.B., Adv. Protein Chem. 47 (1995), 83–229.
2. [2] Camilloni, C., Rocco, A.G., Eberini, I., Gianazza, E., Broglia, R.A., Tiana, G., Biophys. J. 94 (2008), 4654–4661.
3. [3] Fan, D.J., Ding, Y.W., Zhou, J.M., Biochim. Biophys. Acta 6 (2009), 944–952.
4. [4] Dubey, V.K., Jagannadham, M., Biochemistry 42 (2003), 12287–12297.
5. [5] Kumar, Y., Muzammil, S., Tayyab, S., J. Biochem. 138 (2005), 335–341.
6. [6] Pace, C.N., Trevino, S., Prabhakaran, E., Scholtz, J.M., Philos. Trans. R. Soc. Lond. B Biol. Sci. 359 (2004), 1225–1234.
7. [7] Goto, Y., Takahashi, N., Fink, A.L., Biochemistry 29 (1990), 3480–3488.
8. [8] Dolgikh, D.A., Gilmanshin, R.I., Brazhnikov, E.V., Bychkova, V.E., Semisotnov, G.V., Venyaminov, S., Ptitsyn, O.B., FEBS Lett. 136 (1981), 311–315.
9. [9] Goto, Y., Fink, A.L., Biochemistry 28 (1989), 945–952.
10. [10] Semisotnov, G.V., Rodionova, N.A., Razgulyaev, O.I., Uversky, V.N., Gripas, A.F., Gilmanshin, R.I., Biopolymers 31 (1991), 119–128.
11. [11] Couthon, F., Clottes, E., Ebel, C., Vial, C., Eur. J. Biochem. 234 (1995), 160–170.
12. [12] Celej, M.S., Montich, G.G., Fidelio, G.D., Protein Sci. 12 (2003), 1496–1506.
13. [13] Brandts, J.F., Lin, L.N., Biochemistry 29 (1990), 6927–6940.
14. [14] Shrake, A., Ross, P.D., J. Biol. Chem. 265 (1990), 5055–5059.
15. [15] Shrake, A., Ross, P.D., Biopolymers 32 (1992), 925–940.
16. [16] Kandeel, M., Nakanishi, M., Ando, T., El-Shazly, K., Yosef, T., Ueno, Y., Kitade, Y., Mol. Biochem. Parasitol. 159 (2008), 130–133.
17. [17] Sekulic, N., Shuvalova, L., Spangenberg, O., Konrad, M., Lavie, A., J. Biol. Chem. 277 (2002), 30236–30243.
18. [18] Blaszczyk, J., Li, Y., Yan, H., Ji, X., J. Mol. Biol. 307 (2001), 247–257.
19. [19] Ping, J., Hao, P., Li, Y.X., Wang, J.F., BioMed Res. Int., 2013, 2013, 628536.
20. [20] Gupta, S., Yadav, S., Singh, N., Verma, A., Siddiqi, I., Saxena, J.K., Parasitology 141 (2014), 1341–1352.
21. [21] Agarwal, K., Miech, R., Parks, R., Methods Enzymol. 51 (1978), 483–490.
22. [22] Eftink, M.R., Ghiron, C.A., Anal. Biochem. 114 (1981), 199–227.
23. [23] Suryanarayanan, V., Singh, S.K., J. Recept. Signal Transduction 35 (2015), 370–380.
24. [24] Tripathi, S.K., Singh, S.K., Mol. Biosyst. 10 (2014), 2189–2201.
25. [25] Plomer, J.J., Gafni, A., Biochim. Biophys. Acta 1122 (1992), 234–242.
26. [26] Alam, P., Rabbani, G., Badr, G., Badr, B.M., Khan, R.H., Cell Biochem. Biophys. 71 (2015), 1199–1206.
27. [27] Hayashi, S., Nakamura, S., Biochim. Biophys. Acta 657 (1981), 40–51.
28. [28] Gimenez-Gallego, Eur. J. Biochem. 246 (1997), 328–335.
29. [29] Pawar, S., Deshpande, V., Eur. J. Biochem. 267 (2000), 6331–6338.
30. [30] Silva, N. Jr., Gratton, E., Mei, G., Rosato, N., Rusch, R., Finazzi-Agro, A., Biophys. Chem. 48 (1993), 171–182.
31. [31] Louzada, P.R., Sebollela, A., Scaramello, M.E., Ferreira, S.T., Biophys. J. 85 (2003), 3255–3261.
32. [32] Bhatt, A.N., Khan, M.Y., Bhakuni, V., Protein Sci. 13 (2004), 2184–2195.
33. [33] Ahmad, B., Muteeb, G., Alam, P., Varshney, A., Zaidi, N., Ishtikhar, M., Badr, G., Mahmoud, M.H., Khan, R.H., Int. J. Biol. Macromol. 75 (2015), 447–452.
34. [34] Abdelhameed, A.S., Alam, P., Khan, R.H., J. Biomol. Struct. Dyn. 34 (2016), 2037–2044.
35. [35] Chipman, D.M., Grisaro, V., Sharon, N., J. Biol. Chem. 242 (1967), 4388–4394.
36. [36] Hosen, M.J., Zubaer, A., Thapa, S., Khadka, B., De Paepe, A., Vanakker, O.M., PLoS One, 9, 2014, e102779.
37. [37] Alam, P., Chaturvedi, S.K., Anwar, T., Siddiqi, M.K., Ajmal, M.R., Badr, G., Mahmoud, M.H., Khan, R.H., J. Lumin. 164 (2015), 123–130.
38. [38] Du, X., Li, Y., Xia, Y.L., Ai, S.M., Liang, J., Sang, P., Ji, X.L., Liu, S.Q., Int. J. Mol. Sci., 17, 2016, 144.
39. [39] Vonrhein, C., Schlauderer, G.J., Schulz, G.E., Structure 3 (1995), 483–490.