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Principles of Inter-Amino-Acid Recognition Revealed by Binding Energies between Homogeneous Oligopeptides

  • Author(s): Du, Huiwen
  • Hu, Xiaoyu
  • Duan, Hongyang
  • Yu, Lanlan
  • Qu, Fuyang
  • Huang, Qunxing
  • Zheng, Wangshu
  • Xie, Hanyi
  • Peng, Jiaxi
  • Tuo, Rui
  • Yu, Dan
  • Lin, Yuchen
  • Li, Wenzhe
  • Zheng, Yongfang
  • Fang, Xiaocui
  • Zou, Yimin
  • Wang, Huayi
  • Wang, Mengting
  • Weiss, Paul S
  • Yang, Yanlian
  • Wang, Chen
  • et al.

Published Web Location

https://pubs.acs.org/doi/pdf/10.1021/acscentsci.8b00723
No data is associated with this publication.
Abstract

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 (ΔG 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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