Parole chiave: Deamidation, Folding, Isoaspartate, Mass Spectrometry, Protein Structure-Function, Ribonuclease A, Amino Acid Substitution, Article, Deamination, Disulfide Bond, Enzyme Analysis, Enzyme Structure, Priority Journal, Protein Folding, Structure Analysis, Animals, Cattle, Glutathione, Hydrogen Bonding, Kinetics, Oxidation-Reduction, Pancreatic,
Affiliazioni:
Dipartimento di Chimica, Università degli Studi di Salerno, Salerno, Italy Centro di Studio di Biocristallografia CNR, c/o Dipartimento di Chimica, Università degli Studi di Napoli Federico II, Italy Centro Internazionale di Servizi Spettrometria di Massa, CNR-Università di Napoli, Italy CEINGE, Biotecnologie Avanzate, Scrl, Napoli, Italy
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Anfinsen, C. B., Principles that govern the folding of protein chains (1973) Science, 181, pp. 223-23
Creighton, T. E., Toward a better understanding of protein folding pathways (1988) Proc Natl Acad Sci USA, 85, pp. 5082-5086
Gray, W. R., Disulphide structures of highly bridged peptides: A new strategy for analysis (1993) Protein Sci, 2, pp. 1732-1748
Kraulis, P. J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J Appl Crystallogr, 24, pp. 946-950
Montelione, G. T., Scheraga, H. A., Formation of local structures in protein folding (1989) Acc Chem Res, 22, pp. 70-76
Morris, H. R., Pucci, P., A new method for rapid assignment of SS bridges in proteins (1985) Biochem Biophys Res Commun, 126, pp. 1122-1128
Qin, K., Yang, D. -S., Yang, Y., Chishti, M. A., Meng, L. -J., Kretzschmar, H. A., Copper (II) -induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and dearnidation (2000) J Biol Chem, 275, pp. 19121-19131
Raines, R. T., Ribonuclease A (1998) Chem Rev, 98, pp. 1045-1066
Schaffer, S. W., Ahmed, A. K., Wetlaufer, D. B., Salt effects in the glutathione-facilitated reactivation of reduced bovine pancreatic ribonuclease (1975) J Biol Chem, 250, pp. 8483-8486
Volles, M. J., Xu, X., Scheraga, H. A., Distribution of disulfide bonds in the two-disulfide intermediates in the regeneration of bovine pancreatic ribonuclease A: Further insights into the folding process (1999) Biochemistry, 38, pp. 7284-7293
Wedemeyer, W. J., Welker, E., Narayan, M., Scheraga, H. A., Disulfide bonds and protein folding (2000) Biochemistry, 39, pp. 4207-4216
The folding of ribonuclease A (RNase A) has been extensively studied by characterizing the disulfide containing intermediates using different experimental conditions and analytical techniques. So far, some aspects still remain unclear such as the role of the loop 65-72 in the folding pathway. We have studied the oxidative folding of a RNase A derivative containing at position 67 the substitution Asn --> isoAsp where the local structure of the loop 65-72 has been modified keeping intact the C65-C72 disulfide bond. By comparing the folding behavior of this mutant to that of the wild-type protein, we found that the deamidation significantly decreases the folding rate and alters the folding pathway of RNase A. Results presented here shed light on the role of the 65-72 region in the folding process of RNase A and also clarifies the effect of the deamidation on the folding/unfolding processes. On a more general ground, this study represents the first characterization of the intermediates produced along the folding of a deamidated protein.
197 Records (194 escludendo Abstract e Conferenze). Impact factor totale: 729.776 (714.698 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 747.78 (728.737 escludendo Abstract e Conferenze).
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