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. 2016 Sep 5;5(3):19. doi: 10.3390/antib5030019

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© 2016 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).

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Rational design and identification of stabilized C_H1–C_κ. (A) Structural analysis of the C_H1–C_κ interface. The side chains of hydrophobic residues at the interface are shown in slim stick representation. The four amino acid residues lining a void structure are indicated with their side chains shown in a bold ball-and-stick representation; (B) Size-exclusion chromatography of mD1.22-C_H1/m36.4-C_L variants. Proteins were treated with and without 1 mM TCEP (tris(2-carboxyethyl)phosphine) before analysis. The arrows at the top indicate the elution volumes of the molecular mass standards in PBS (pH 7.4): carbonic anhydrase (29 kDa), ovalbumin (44 kDa) and conalbumin (75 kDa).