Report

An Analysis of the Origins of a Cooperative Binding Energy of Dimerization

Science  01 May 1998:
Vol. 280, Issue 5364, pp. 711-714
DOI: 10.1126/science.280.5364.711

You are currently viewing the abstract.

View Full Text

Via your Institution

Log in through your institution

Log in through your institution


Abstract

The cooperativity between binding of cell wall precursor analogs (ligands) to and antibiotic dimerization of the clinically important vancomycin group antibiotics was investigated by nuclear magnetic resonance. When dimerization was weak in the absence of a ligand, the increase in the dimerization constant in the presence of a ligand derived largely from changes associated with tightening of the dimer interface. When dimerization was strong in the absence of a ligand, the increase in the dimerization constant in the presence of a ligand derived largely from changes associated with tightening of the ligand-antibiotic interface. These results illustrate how, when a protein has a loose structure, the binding energy of another molecule to the protein can derive in part from changes occurring within the protein.

  • * To whom correspondence should be addressed. E-mail: dhw1{at}cam.ac.uk

View Full Text

Related Content