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Welfe, Aleksander; Majsterek, Michał

doi:10.1023/a:1022420518609

Cited by 3 publications

(1 citation statement)

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“…This spectrum is also distinct from that of denaturant‐unfolded VH. A similar increase of negative ellipticity in the far‐UV region has been observed at strongly acidic pH for partially unfolded states of the mouse monoclonal antibodies and their Fab fragments [34–36], as well as the isolated CH3 [37] and VL [38,39] domains. Together, these data and our CD spectra indicate that the anti‐ferritin VH domain adopts a non‐native secondary conformation with a significant amount of a β‐sheet structure which is markedly distorted and resembles the structure of immunoglobulins partially unfolded under strongly acidic conditions.…”

Section: Resultssupporting

confidence: 71%

Partially structured state of the functional VH domain of the mouse anti‐ferritin antibody F11

et al. 2002

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An antibody combining site generally involves the two variable domains, VH from the heavy and VL from the light chain. We expressed the individual VH domain of the mouse antihuman ferritin monoclonal antibody F11. The loss of affinity was not dramatic (K a = 4.0U U10 7 M 31 versus 8.6U U10 8 M 31 for the parent antibody) and comparable to that previously observed for other VHs. However, the functional VH domain adopted a partially structured state with a significant amount of distorted secondary and compact yet greatly destabilized tertiary structures, as demonstrated by spectroscopic and calorimetric probes. These data provide the first description for a functional antibody domain that meets all the criteria of a partially structured state. ß 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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Section: Resultssupporting

confidence: 71%