caa a22 4500 47576613X CHVBK 20180406123606.0 cr unu---uuuuu 170329e20000701xx s 000 0 eng 10.1007/s007050070104 doi (NATIONALLICENCE)springer-10.1007/s007050070104 Conformational changes during proteolytic processing of a picornavirus capsid proteins [Elektronische Daten] [M. S. Smyth, A. Trudgett, J. H. Martin, E. M. Hoey, S. J. Martin] Summary.:  We have used synthetic peptide antibodies to probe conformational changes that occur during the cleavage cascade which generates the capsid proteins of a picornavirus. The initial translation product of 97 kDa, the precursor of all four structural proteins, is cleaved to form a 63 kDa fragment which, we show, has significantly different folding characteristics to both its larger parent and its products. We demonstrate that proteolytic cleavages as distant as 520 residues from epitopes confer sufficiently large conformational changes as to render them unrecognisable. To our knowledge, this is the first demonstration of this phenomenon in the picornavirus system. Springer-Verlag/Wien, 2000 Smyth M. S. Department of Biochemistry, University of Leicester, Leicester, U.K., GB aut Trudgett A. School of Biology and Biochemistry, Queen's University of Belfast, Belfast, U.K., GB aut Martin J. H. Division of Biomedical Sciences, School of Health Sciences, University of Wolverhampton, Wolverhampton, U.K., GB aut Hoey E. M. School of Biology and Biochemistry, Queen's University of Belfast, Belfast, U.K., GB aut Martin S. J. School of Biology and Biochemistry, Queen's University of Belfast, Belfast, U.K., GB aut https://doi.org/10.1007/s007050070104 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s007050070104 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Smyth M. S. Department of Biochemistry, University of Leicester, Leicester, U.K., GB aut NATIONALLICENCE 700 1- Trudgett A. School of Biology and Biochemistry, Queen's University of Belfast, Belfast, U.K., GB aut NATIONALLICENCE 700 1- Martin J. H. Division of Biomedical Sciences, School of Health Sciences, University of Wolverhampton, Wolverhampton, U.K., GB aut NATIONALLICENCE 700 1- Hoey E. M. School of Biology and Biochemistry, Queen's University of Belfast, Belfast, U.K., GB aut NATIONALLICENCE 700 1- Martin S. J. School of Biology and Biochemistry, Queen's University of Belfast, Belfast, U.K., GB aut Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer