Selection for improved protein stability by phage display 1 1Edited by J. A. Wells
- 1 November 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 294 (1), 163-180
- https://doi.org/10.1006/jmbi.1999.3196
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- The nature of antibody heavy chain residue H6 strongly influences the stability of a VH domain lacking the disulfide bridgeJournal of Molecular Biology, 1998
- Antibody scFv fragments without disulfide bonds, made by molecular evolutionJournal of Molecular Biology, 1998
- β‐Turn propensities as paradigms for the analysis of structural motifs to engineer protein stabilityProtein Science, 1997
- A phage display system for studying the sequence determinants of protein foldingProtein Science, 1995
- 1.85 Å structure of anti-fluorescein 4-4-20 FabProtein Engineering, Design and Selection, 1995
- In Vitro Assembly of Repertoires of Antibody Chains on the Surface of Phage by RenaturationJournal of Molecular Biology, 1994
- Structural Patterns at Residue Positions 9, 18, 67 and 82 in the VH Framework Regions of Human and Murine ImmunoglobulinsJournal of Molecular Biology, 1993
- X-ray Structures of the Antigen-binding Domains from Three Variants of Humanized anti-p185HER2 Antibody 4D5 and Comparison with Molecular ModelingJournal of Molecular Biology, 1993
- Relative binding properties of fluorescein and 9-hydroxyphenylfuoron (HPF) with murine monoclonal anti-fluorescein antibodiesBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985