Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2017 Mar 16;7:212. doi: 10.1038/s41598-017-00188-7

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2017

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

PMC Copyright notice

Structural parameters of KYE21 and WWWKYE21 in LPS. Bar diagram (left panel) and histogram (right panel) of (a) KYE21 and (b) WWWKYE21, showing important long-range and medium-range αN (i, i + 2/i + 3/i + 4), as well as long range-NOE contacts (i, ≥i + 5) among the backbone-backbone and backbone-side chain resonances found in the trNOESY spectra, used to calculate the bound conformation of the peptides. The bar thickness in the bar diagrams corresponds directly to the NOE intensities. The primary amino acid sequences are provided at the top of the bar diagrams. The histogram depicts the number of NOE constraints used to calculate the bound conformation of the peptides as a function of residue number. The arrowheads in the histogram mark the residues that share long-range contacts with each other.