Stability and Folding of Endoglucanase I (CEL7B) from Humicoia Insolens

References

• Arunachalam U., Kellis J. T. “Folding and stability of endoglucanase III, a single-domain cellulase from Trichoderma reesei”. Biochemistry 1996; 35: 11379–11385
   PubMed Web of Science ®Google Scholar
• Baldwin R. “On-pathway versus off-pathway folding intermediates”. Fold. Des 1996; 1: R1–R8
   Google Scholar
• Clarke J., Fersht A. R. “Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation”. Biochemistry 1993; 32: 4322–4329
   PubMed Web of Science ®Google Scholar
• Clarke A. R., Waltho J. P. “Protein folding pathways and intermediates”. Curr. Opin. Biotech 1997; 8: 400–410
   PubMed Web of Science ®Google Scholar
• Creighton T. E. Proteins. Structures and Molecular Properties. Freeman, New York 1993
   Google Scholar
• Davies G. J., Dodson G. G., Hubbard R. E., Tolley S. P., Dauter Z., et al. “Structure and function of endoglucanase V”. Nature 1993; 365: 362–364
   PubMed Web of Science ®Google Scholar
• Elove G. A., Chaffotte A. F., Roder H., Goldberg M. E. “Early steps in cytochrome-c folding probed by time-resolved circular dichroism and fluorescence spectroscopy”. Biochemistry 1992; 31: 6876–6883
   PubMed Web of Science ®Google Scholar
• Fersht A. R., Matouschek A., Serrano L. “The folding of an enzyme I: theory of protein engineering analysis of stability and pathway of protein folding”. J. Mol. Biol 1992; 224: 771–782
   PubMed Web of Science ®Google Scholar
• Goto Y., Takahashi N., Fink A. L. “Mechanism of acid-induced folding of proteins”. Biochemistry 1990; 29: 3480–3488
   PubMed Web of Science ®Google Scholar
• Guijarro J. I., Jackson M., Chaffotte A. F., Delepierre M., Mantsch H. H., et al. “Protein folding intermediates with rapidly exchangeable amide protons contain authentic hydrogen-bonded secondary structures”. Biochemistry 1995; 34: 2998–3008
   PubMed Web of Science ®Google Scholar
• Henrissat B., Bairoch A. “New families in the classification of glycosyl hydrolases based on amino acid sequence similarities”. Biochem. J 1993; 293: 781
   PubMed Web of Science ®Google Scholar
• Itzhaki L. S., Otzen D. E., Fersht A. R. “The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering: evidence for a nucleation-condensation mechanism for protein folding”. J. Mol. Biol 1995; 254: 260–288
   PubMed Web of Science ®Google Scholar
• Kitamura S., Sturtevant J. M. “A scanning calorimetric study of the thermal denaturation of the lysozyme of phage T4 and the Arg96His mutant form thereof. Biochemistry 1989; 28: 3788–3792
   PubMed Web of Science ®Google Scholar
• Lange N. K. Trichoderma reesei cellulases and other hydrolases, P. Suominen, T. Reinikainen. Foundation for Biotechnical and Industrial Fermentation, Helsinki 1993; 263–272
   Google Scholar
• Lin L. H., Brandts J. F. “Evidence for the existence of three or more slow phases in the refolding of RNase A and some characteristics of the phases”. Biochemistry 1987; 26: 3537–3543
   PubMed Web of Science ®Google Scholar
• Lopez-Hemandes I., Serrano L. “Structure of the transition state for folding of the 129-amino acid protein Che Y resembles that of the smaller protein CI2”. Fold. Des 1996; 1: 43–55
   PubMedGoogle Scholar
• MacKenzie K. R., Prestegaard J. H., Engelman DM. “A transmembrane helix dimer: structure and implications”. Science 1997; 276: 131–133
   PubMed Web of Science ®Google Scholar
• MacKenzie L. F., Sulzenbacher G., Divne C, Jones T. A., Wöldike H. F., et al. “Crystal structure of the family 7 endoglucanase I (Cel7B) from Humicola insolens at 2.2Å resolution and identification of the catalytic nucleophile by trapping of the covalent glycosyl-enzyme intermediate”. Biochem. J 1998; 335: 409
   PubMed Web of Science ®Google Scholar
• Makhatadze G. I., Privalov PL. “Heat capacity of proteins I. partial molar heat capacity of individual amino acids in aqueous solution: hydration effect”. J. Mol. Biol 1990; 213: 375–384
   PubMed Web of Science ®Google Scholar
• Matouschek A., Kellis J. T., Serrano L., Bycroft M., Fersht A. R. “Transient folding intermediates characterized by protein engineering”. Nature 1990; 346: 440–445
   PubMed Web of Science ®Google Scholar
• Neri D., Billeter M., Wider G., Wüthrich K. “NMR determination of residual structure in a urea-denatured protein, the 434-repressor”. Science 1992; 257: 1559–1563
   PubMed Web of Science ®Google Scholar
• Otzen D. E., Christensen L., Schülein M. “A comparative study of the unfolding of EGV in denaturant and surfactant”. Prot. Sci 1999a; 8: 1878–1887
   PubMed Web of Science ®Google Scholar
• Otzen D. E., Kristensen O., Proctor M., Oliveberg M. “Structural changes in the transition state of protein folding: an alternative interpretation of curved chevron plots”. Biochemistry 1999b; 38: 6499–6511
   PubMed Web of Science ®Google Scholar
• Pace C. N., Alston R. W., Shaw K. L. “Charge-charge interactions influence the denatured state ensemble and contribute to protein stability”. Prot. Sci 2000; 9: 1395–1398
   PubMed Web of Science ®Google Scholar
• Parker M. J., Spencer J., Clarke A. R. “An integrated kinetic analysis of intermediates and transition states in protein folding reactions”. J. Mol. Biol 1995; 253: 771–786
   PubMed Web of Science ®Google Scholar
• Privalov PL. “Stability of proteins”. Adv. Prot. Chem 1979; 33: 167–236
   PubMedGoogle Scholar
• Privalov PL. “Scanning microcalorimetry in studying temperature-induced changes in proteins”. Methods Enzymol 1987; 131: 4–51
   Google Scholar
• Radford S. E., Dobson CM, Evans PA. “The folding of hen lysozyme involves partially structured intermediates and multiple pathways”. Nature 1992; 358: 302–307
   PubMed Web of Science ®Google Scholar
• Schou C, Rasmussen G., Kaltoft M.-B., Henrissat B., Schüein M. “Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodextrins by nine cellulases”. Eur. J. Biochem 1993; 217: 947–953
   PubMedGoogle Scholar
• Schülein M. “Enzymatic properties of cellulases from Humicola insolens”. J. Biotechnol 1997; 57: 71–81
   PubMed Web of Science ®Google Scholar
• Schülein M. “Kinetics of fungal cellulases”. Biochem. Soc. Trans 1998; 26: 164–167
   PubMed Web of Science ®Google Scholar
• Schülein M., Kauppinen M. S., Lange L., Lassen S. F., Andersen L. N., . “Characterization of fungal cellulases for fiber modification”. Enzyme applications in Fiber Processing, ACS Symposium Series, K.-E. L. Eriksson, A. Cavaco-Paulo, et al. American Chemical Society, Washington 1998; 66–74
   Google Scholar
• Silow M., Oliveberg M. “High-energy channelling in protein folding”. Biochemistry 1997; 36: 7633–7637
   PubMed Web of Science ®Google Scholar
• Tanford C. “Protein denaturation. Part C. Theoretical models for the mechanism of denaturation”. Adv. Prot. Chem 1970; 24: 1–95
   PubMedGoogle Scholar
• Tomme P., Warren R. A.J., Gilkes N. R. “Cellulose hydrolysis by bacteria and fungi”. Adv. Microb. Physiol 1995; 37: 1–81
   PubMedGoogle Scholar
• Wong K. B., Clarke J., Bond C. J., Neira J. L., Freund S. M., et al. “Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding”. J. Mol. Biol 2000; 296: 1257–1282
   PubMed Web of Science ®Google Scholar