Secondary structure determines electron transport in peptides

• 成果类型: Article
• 署名作者: Samajdar, Rajarshi; Meigooni, Moeen; Yang, Hao; Li, Jialing; Liu, Xiaolin; Jackson, Nicholas E.; Mosquera, Martin A.; Tajkhorshid, Emad; Schroeder, Charles M.
• 署名单位: University of Illinois System; University of Illinois Urbana-Champaign; University of Illinois System; University of Illinois Urbana-Champaign; University of Illinois System; University of Illinois Urbana-Champaign; University of Illinois System; University of Illinois Urbana-Champaign; University of Illinois System; University of Illinois Urbana-Champaign; Montana State University System; Montana State University Bozeman; University of Illinois System; University of Illinois Urbana-Champaign; University of Illinois System; University of Illinois Urbana-Champaign
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-8595
• DOI: 10.1073/pnas.2403324121
• 发表日期: 2024-08-06
• 关键词: tunneling pathways; charge-transport; molecular junctions; side-chains; DYNAMICS; validation; TRANSITION; simulation; distance; length

摘要

Proteins play a key role in biological electron transport, but the structure-function relationships governing the electronic properties of peptides are not fully understood. Despite recent progress, understanding the link between peptide conformational flexibility, hierarchical structures, and electron transport pathways has been challenging. Here, we use single- molecule experiments, molecular dynamics (MD) simulations, nonequimachine learning to understand the role of secondary structure on electron transport in peptides. Our results reveal a two- state molecular conductance behavior for peptides across several different amino acid sequences. MD simulations and Gaussian mixture modeling are used to show that this two- state molecular conductance behavior arises due to the conformational flexibility of peptide backbones, with a high- conductance state arising due to a more defined secondary structure (beta turn or 310 helices) and a the importance of helical conformations on electron transport in peptides. Conformer of intramolecular hydrogen bonding distances along peptide backbones. Molecular concalculations, and the results are in reasonable qualitative agreement with experiments. provides broad avenues for understanding the electronic properties of proteins.