The intrinsic contributions of tyrosine, serine, glycine and arginine to the affinity and specificity of antibodies.

By S. Birtalan, Yingnan Zhang, Frederic A. Fellouse, Lihua Shao, G. Schaefer, S. Sidhu. 2008

247 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Antibody i-Patch prediction of the antibody binding site improves rigid local antibody-antigen docking. (2013, result): “These high contact propensities of tyrosine and tryptophan in antibodies are in agreement with earlier theoretical (Mian et al., 1991) and experimental (Fellouse et al., 2005; Birtalan et al., 2008) findings.”
Protein–protein interaction and quaternary structure (2008, background): “Birtalan et al. (2008) have recently analyzed the role of arginines and tyrosines at the antigen-combining site of antibodies, where they are the most abundant residue types.”
Nonspecificity in a nonimmune human scFv repertoire (2017, background): “Of the residues exposed in the loop, in general tyrosine and serine have not been shown to increase nonspecific binding.(9,10)”
Generation and analyses of human synthetic antibody libraries and their application for protein microarrays. (2016, background): “…CDR-L3 were allowed a much more complex chemical diversity based on the knowledge of what is commonly found in natural antibodies of CDR-H3 (Zemlin et al., 2003) and on experiences from earlier synthetic antibody library designs (Fellouse et al., 2007; Birtalan et al., 2008; Persson et al., 2013).”