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Journal of Molecular Biology|June 9, 2001
The influence of the buried glutamine or glutamate residue in position 6 on the structure of immunoglobulin variable domainsA Honegger, A PlückthunJournal of Molecular Biology|June 9, 2001
Yet another numbering scheme for immunoglobulin variable domains: an automatic modeling and analysis toolA Honegger, A PlückthunJournal of Molecular Biology|October 14, 1998
Reproducing the natural evolution of protein structural features with the selectively infective phage (SIP) technology. The kink in the first strand of antibody kappa domainsS Spada, A Honegger, A PlückthunJournal of Molecular Biology|November 11, 1999
Selection for improved protein stability by phage displayS Jung, A Honegger, A PlückthunJournal of Molecular Biology|January 17, 1997
A natural antibody missing a cysteine in VH: consequences for thermodynamic stability and foldingK Proba, A Honegger, A PlückthunProtein Engineering|April 1, 1997
Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragmentL Nieba, A Honegger, C Krebber, et al.Journal of Molecular Biology|February 19, 1998
Antibody scFv fragments without disulfide bonds made by molecular evolutionK Proba, A Wörn, A Honegger, et al.FEBS Letters|November 14, 1997
Affinity and folding properties both influence the selection of antibodies with the selectively infective phage (SIP) methodologyG Pedrazzi, F Schwesinger, A Honegger, et al.Proceedings of the National Academy of Sciences of the United States of America|January 3, 2001
Tailoring in vitro evolution for protein affinity or stabilityL Jermutus, A Honegger, F Schwesinger, et al.Biochemistry|June 25, 1996
Folding nuclei of the scFv fragment of an antibodyC Freund, A Honegger, P Hunziker, et al.Pageof 18