Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

A synthetic mimic of protein inner space: Buried polar interactions in a deep water-soluble host

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Butterfield, S. M.
  • Rebek Jr., Julius

publication date

  • December 2006

journal

  • Journal of the American Chemical Society  Journal

abstract

  • A deep water-soluble cavitand was functionalized with a carboxylic acid directed toward the hydrophobic interior of the host. The buried salt-bridge interaction formed with a quinuclidium cationic guest was determined to be worth -3 kcal/mol using a free energy cycle. The strength of the interaction correlates well with buried salt bridges in proteins, indicating that the cavitand interior mimics the hydrophobic inner space of proteins.

subject areas

  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Proteins
  • Solubility
  • Water
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja0663374

PubMed ID

  • 17131990
scroll to property group menus

Additional Document Info

start page

  • 15366

end page

  • 15367

volume

  • 128

issue

  • 48

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support