1999
DOI: 10.1016/s0022-0248(98)00820-3
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Packing motifs as predictors of the propensity of antibody fragments to crystallize

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Cited by 7 publications
(1 citation statement)
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“…In this review, we will discuss the structures of the last two ß-strands, designated F (3-2) and G (3-3), and the turn, connecting these strands. The F-to-G loop is the most solvent exposed region of CL and CH1 domains of an Fab and its structure has been observed to vary for different isotypes of L and H chains [36]. For example, in Ï-chains the F-to-G loop forms a classical ß-hairpin structure, while in Î-chains the turn connecting the two ß-strands is expanded by two additional residues and a proline residue.…”
Section: General Features Of Immunoglobulin V and C Domainsmentioning
confidence: 99%
“…In this review, we will discuss the structures of the last two ß-strands, designated F (3-2) and G (3-3), and the turn, connecting these strands. The F-to-G loop is the most solvent exposed region of CL and CH1 domains of an Fab and its structure has been observed to vary for different isotypes of L and H chains [36]. For example, in Ï-chains the F-to-G loop forms a classical ß-hairpin structure, while in Î-chains the turn connecting the two ß-strands is expanded by two additional residues and a proline residue.…”
Section: General Features Of Immunoglobulin V and C Domainsmentioning
confidence: 99%