Monoclonal Antibody Epitope Mapping Describes Tailspike β-Helix Folding and Aggregation Intermediates
Open Access
- 1 June 2005
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 280 (24) , 23032-23040
- https://doi.org/10.1074/jbc.m501963200
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- Mapping Aβ Amyloid Fibril Secondary Structure Using Scanning Proline MutagenesisJournal of Molecular Biology, 2004
- Protein folding and misfoldingNature, 2003
- Molecular Chaperones in the Cytosol: from Nascent Chain to Folded ProteinScience, 2002
- Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavageJournal of Molecular Biology, 1997
- Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodiesProtein Science, 1997
- Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chainsProtein Science, 1995
- Conformational change in the N-terminal domain of the Escherichia coli tryptophan synthase β2 subunit induced by its interactions with monoclonal antibodiesResearch in Immunology, 1990
- Phage P22 tail protein: gene and amino acid sequenceBiochemistry, 1982
- Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike proteinJournal of Molecular Biology, 1981