References
- Schymkowitz JWH, Rousseau F, Serrano L. Commentary: Surfing on protein folding energy landscape. Proc Natl Acad Sci USA 2002; 99: 15846–15848
- Wu JW, Wang ZX, Zhou JM. Three state kinetic analysis of chinese hamster dihydrofolate reductase unfolding by guanidine hydrochloride. Biochim Biophys Acta 1997; 1343: 107–116
- Onuchic JN, Wolynes PG, Luthey-Schulten Z, Socci ND. Towards an outline of the topography of a realistic protein folding funnel. Proc Natl Acad Sci USA 1995; 92: 3626–3630
- Dill KA, Chan HS. From Levinthal to pathways to funnels. Nat Struct Biol 1997; 4: 10–19
- Karplus M. The Levinthal paradox: Yesterday and today. Folding Des 1997; 2: S69–S75
- Dill KA. Polymer principles and protein folding. Protein Sc. 1999; 8: 1166–1180
- Onuchic JN, Socci ND, Luthey-Schulten Z, Wolynes PG. Protein folding funnels: The nature of the transition state ensemble. Folding Des 1996; 1: 441–450
- Shea JE, Onuchic JN, Brooks CL, III. Exploring the origins of topological frustration: Design of a minimally frustrated model of fragment B of a protein A. Proc Natl Acad Sci USA 1999; 96: 12512–12517
- Tsai C-J, Ma B, Sham YY, Kumar S, Nussinov R. Short review: Structured disorder and conformational selection. Prot Struct Funct Genet 2001; 44: 418–427
- Stryer L. Biochemistry. W.H. Freeman and Company, New York 1982; 15–16
- Nelson DL, Cox MM. Lehninger: Principles of biochemistry. Worth Publishers, New York 2000, p 90-1; 159–61; 192
- Aghajanian SA, Martin SR, Engel PC. Urea induced inactivation and denaturation of clostridial glutamate dehydrogenase: The absence of stable dimeric or trimeric intermediates. Biochem J 1995; 311: 905–910
- Xiao J, Liang SH, Tsou CL. Inactivation before significant conformational change during denaturation of papain by guanidine hydrochloride. Biochim Biophys Acta 1993; 1164: 54–60
- Wang ZX, Wu JW, Tsou CL. The inactivation kinetics of papain by guanidine hydrochloride: A re-analysis. Biochim Biophys Acta 1998; 1388: 84–92
- Chazzara S, Cabanes J, Escribano J, García-Carmona F. Kinetic study of the suicide inactivation of latent polyphenoloxidase from iceberg lettuce (Lactuca sativa) induced by 4-tert-butylcatechol in the presence of SDS. Biochim Biophys Acta 1997; 1339: 297–303
- Wetlaufer DB, Xie Y. Control of aggregation in protein refolding: A variety of surfactants promote renaturation of carbonic anhydrase II. Protein Sci 1995; 4: 1535–1543
- Pande VS, Rokhsar DS. Is the molten globule a third phase of proteins?. Proc Natl Acad Sci USA 1998; 95: 1490–1494
- Tian WX, Tsou CL. Determination of the rate constant of enzyme modification by measuring the substrate reaction in the presence of the modifier. Biochemistry 1982; 21: 1028–1032
- Sasso S, Protasevich I, Gill R, Makarov A, Briand C. Thermal denaturation of bacterial and bovine dihydrofolate reductases and their complexes with NADPH, trimethoprin and methotrexate. J Biomol Struct Dynam 1995; 12: 1023–1032
- Kornilaev BA, Kurganov BI, Eronina TB, Livanona NB. Thermal inactivation of muscle phosphorylase B: Protective effects of specific ligands. Biochem Mol Biol Int 1996; 38: 921–927
- Arakawa T, Bhat R, Timasheff S. Preferential interactions determine protein solubility in three-componentsolutions: The MgCl2 system. Biochemistry 1990; 29: 1914–1923
- Qu Y, Bolen CL, Bolen DW. Osmolytes-driven contraction of a random coil protein. Proc Natl Acad Sci USA 1998; 95: 9268–9273
- Tompa P, Szász C, Buday L. Structural disorder throws new light on moonlighting. Trends Biochem Sci 2005; 30: 484–489
- Chilaka FC, Okeke C, Adaikpoh E. Ligand-induced thermal stability in β-galactosidase from the seeds of the black bean, Kestingeilla geocarpa. Process Biochem 2002; 38: 143–149
- Bouranis DL, Niavis LA. Cell wall metabolism in growing and ripening store fruits. Plant Cell Physiol 1992; 33: 999–1008
- Ali ZM, Armugen S, Lazan H. β-Galactosidase and its significance in ripening mango fruits. Phytochem 1995; 38: 1109–1114
- Fukuda MN, Fukuda M, Hakamori SI. Cell surface modification by endo-galactosidase. J Biol Chem 1979; 254: 5458–5465
- Hibachi F, Hata J, Mitra M, Dha M, Harmata M, Sun P, Smith D. Purification and characterization of a coffee canephora α-galactosidase enzyme. Biochem Biophys Res Commun 1991; 181: 180–184
- Kornfeld R, Kornfeld S. Structure of glycoproteins and their oligosaccharides. Biochemistry of glycoproteins and proteoglycans, WJ Lennarz. Plenum Press, New York 1980; 1–34
- Biswas TK. Characterization of β-galactosidase from the germinating seeds of Vigna sinensis. Phytochem 1987; 26: 359–364
- Sekimata M, Ogura K, Tsumuraya Y, Hashimoto Y, Yamaoto S. A β-galactosidase from radish (Raphanus sativus L) seeds. Plant Physiol 1989; 90: 567–574
- Konno H, Tsumuki H. Purifcation of a β-galactosidase from rice shoots and its involvement in hydrolysis of the natural substrate in cell walls. Physiol Plant 1993; 89: 40–47
- Lowry OH, Rosenbrough NJ, Farr AC, Randall RJ. Protein measurement with folin-phenol reagent. J Biol Chem 1951; 193: 265–275
- Frieden C. Kinetic aspects of regulation of metabolic processes. The hysteric enzyme concept. J Biol Chem 1970; 245: 5788–5799
- Jaffe EK. Morpheeins-a new structural paradigm for allosteric regulation. Trends Biochem Sci 2005; 30: 490–497
- Reynolds JA, Tanford C. The gross conformation of protein-sodium dodecyl sulfate complexes. J Biol Chem 1970; 245: 5161–5165
- Moore BM, Flurkey WH. Sodium dodecyl sulfate activation of a plant polyphenoloxidase. Effect of sodium dodecyl sulfate on enzymatic and physical characteristics of purified broad bean polyphenoloxidase. J Biol Chem 1990; 265: 4982–4988
- Kuwajima K. Protein folding in vitro. Curr Opin Biotechnol 1992; 3: 462–467
- Shastry MCR, Agashe VR, Udgaonkar JB. Quantitative analysis of the kinetics of denaturation and renaturation of barstar in the folding transition zone. Protein Sci 1994; 3: 1409–1417
- Kim PS, Baldwin RL. Intermediates in the folding reactions of small proteins. Annu Rev Biochem 1990; 59: 631–660
- Mathews CR. Pathways of protein folding. Annu Rev Biochem 1993; 62: 653–683
- Zhang Y-L, Zhou J-M, Tsou CL. Inactivation precedes conformational change during during thermal denaturation of adenylate kinase. Biochem Biophys Acta 1993; 1164: 61–67
- Schreiber G, Fersht AR. The refolding of cis- and trans- peptidyl prolyl isomers of barstar. Biochemistry 1993; 32: 5145–5150
- Jeffery CJ. Moonlighting proteins. Trends Biochem Sci 1999; 24: 8–11
- Jeffery CJ. Multifunctional proteins: Examples of gene sharing. Ann Med 2003; 35: 28–35
- Jeffery CJ. Molecular mechanisms for multitasking: Recent crystal structures of moonlighting proteins. Curr Opin Struct Biol 2004; 14: 663–668
- Price NC. Review: Conformational issues in the characterization of proteins. Biotechnol Appl Biochem 2000; 31: 29–40