Principles of Inter-Amino-Acid Recognition Revealed by Binding Energies between Homogeneous Oligopeptides
Author(s) -
Huiwen Du,
XiaoYu Hu,
Hongyang Duan,
Lanlan Yu,
Fuyang Qu,
Qunxing Huang,
Wangshu Zheng,
H.-L. Xie,
Jiaxi Peng,
Rui Tuo,
Dan Yu,
YuChen Lin,
Wenzhe Li,
Yongfang Zheng,
Xiaocui Fang,
Yimin Zou,
Huayi Wang,
Mengting Wang,
Paul S. Weiss,
Yanlian Yang,
Chen Wang
Publication year - 2019
Publication title -
acs central science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.893
H-Index - 76
eISSN - 2374-7951
pISSN - 2374-7943
DOI - 10.1021/acscentsci.8b00723
Subject(s) - oligopeptide , homogeneous , amino acid , computational biology , chemistry , combinatorial chemistry , biochemistry , biology , peptide , statistical physics , physics
We have determined the interaction strengths of the common naturally occurring amino acids using a complete binding affinity matrix of 20 × 20 pairs of homo-octapeptides consisting of the 20 common amino acids between stationary and mobile states. We used a bead-based fluorescence assay for these measurements. The results provide a basis for analyzing specificity, polymorphisms, and selectivity of inter-amino-acid interactions. Comparative analyses of the binding energies, i.e., the free energies of association (Δ G A ), reveal contributions assignable to both main-chain-related and side-chain-related interactions originating from the chemical structures of these 20 common amino acids. Side-chain-side-chain and side-chain-main-chain interactions are found to be pronounced in an identified set of amino acid pairs that determine the basis of inter-amino-acid recognition.
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