Importance of structural tightening, as opposed to partially bound States, in the determination of chemical shift changes at noncovalently bonded interfaces

J Am Chem Soc. 2004 Nov 3;126(43):14267-72. doi: 10.1021/ja047198y.

Abstract

Two models (A and B) have been proposed to account for decreased downfield chemical shifts of a proton bound by noncovalent interactions at a ligand/antibiotic interface as the number of ligand/antibiotic interactions is decreased. In model A, the proton involved in the noncovalent bond suffers a smaller downfield shift because the bond is, with a relatively large probability, broken, and not because it is longer. In model B, the proton involved in the noncovalent bond suffers a smaller downfield shift because the bond is longer, and not because it is, with a relatively large probability, broken. We show that model A cannot account for the chemical shift changes. Model B accounts for the process of positively cooperative binding, in which noncovalent bonds are reduced in length and thereby increase the stability of the organized state.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Hydrogen Bonding
  • Kinetics
  • Models, Chemical*
  • Nuclear Magnetic Resonance, Biomolecular
  • Oligopeptides / chemistry*
  • Oligopeptides / metabolism
  • Ristocetin / chemistry*
  • Ristocetin / metabolism
  • Thermodynamics
  • Vancomycin / analogs & derivatives*
  • Vancomycin / chemistry*
  • Vancomycin / metabolism

Substances

  • Oligopeptides
  • chloroeremomycin
  • Ristocetin
  • ristocetin A
  • lysyl-alanyl-alanine
  • Vancomycin