Significant Differences in Physicochemical Properties of Human Immunoglobulin Kappa and Lambda CDR3 Regions
Catherine Townsend; Julie Laffy; Bryan Wu; Joselli Silva O’Hare; Victoria Martin; David Kipling; Franca Fraternali; Deborah K. Dunn‐Walters · 2016 · Frontiers in Immunology
WASTE classifies this as Negative / Null Result Report · AI classification, approximate
The study found no significant effect — useful as a negative control or null benchmark for your own design.
Abstract
Antibody variable regions are composed of a heavy and a light chain, and in humans, there are two light chain isotypes: kappa and lambda. Despite their importance in receptor editing, the light chain is often overlooked in the antibody literature, with the focus being on the heavy chain complementarity-determining region (CDR)-H3 region. In this paper, we set out to investigate the physicochemical and structural differences between human kappa and lambda light chain CDR regions. We constructed a dataset containing over 29,000 light chain variable region sequences from IgM-transcribing, newly f
Abstract by Catherine Townsend; Julie Laffy; Bryan Wu; Joselli Silva O’Hare; Victoria Martin; David Kipling; Franca Fraternali; Deborah K. Dunn‐Walters, Frontiers in Immunology (2016) — licensed CC BY 4.0.
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Metadata source: OpenAlex · DOI 10.3389/fimmu.2016.00388
