A Theoretical Study of the Binding of Small Molecules to a Polymerizing Protein System. A Model for Allosteric Effects*

LW Nichol, WJH Jackson, DJ Winzor - Biochemistry, 1967 - ACS Publications
LW Nichol, WJH Jackson, DJ Winzor
Biochemistry, 1967ACS Publications
LW Nicholf, WJH Jacksonf, and DJ WinzorJ abstract: Previously established concepts of
multiple equilibria have been applied to a system in which a protein monomer coexists with
a single higher polymer and both bind a low molecular weight solute (S). The treatment
permits the number of binding sites permole of monomer and polymer to assume any
integral values (including zero), but assumes that sites within a mo-lecular entity are
equivalent with regard to binding, ex-cept for a statistical effect. An equation is derived which …
LW Nicholf, W. J. H. Jacksonf, and D. J. WinzorJ abstract: Previously established concepts of multiple equilibria have been applied to a system in which a protein monomer coexists with a single higher polymer and both bind a low molecular weight solute (S). The treatment permits the number of binding sites permole of monomer and polymer to assume any integral values (including zero), but assumes that sites within a mo-lecular entity are equivalent with regard to binding, ex-cept for a statistical effect. An equation is derived which relates the free equilibrium concentration of S in any equilibrium mixture to a binding function, r, defined on a weight-concentration scale as the concentration of S bound divided bythe initial protein concentration. It is shown that equations of the same form describe binding in other types of systems, including those involving isomerization of the protein and a system in which a series of polymers coexist in equilibrium. In the special case where no binding sites are lost in successive polymeriza-tion reactions and the intrinsic binding constants are
ACS Publications
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