The linkage between protein folding and functional cooperativity: Two sides of the same coin?

Irene Luque, Stephanie A. Leavitt, Ernesto I Freire

Research output: Contribution to journalArticle

Abstract

During the course of their biological function, proteins undergo different types of structural rearrangements ranging from local to large-scale conformational changes. These changes are usually triggered by their interactions with small-molecular-weight ligands or other macromolecules. Because binding interactions occur at specific sites and involve only a small number of residues, a chain of cooperative interactions is necessary for the propagation of binding signals to distal locations within the protein structure. This process requires an uneven structural distribution of protein stability and cooperativity as revealed by NMR-detected hydrogen/deuterium exchange experiments under native conditions. The distribution of stabilizing interactions does not only provide the architectural foundation to the three-dimensional structure of a protein, but it also provides the required framework for functional cooperativity. In this review, the statistical thermodynamic linkage between protein stability, functional cooperativity, and ligand binding is discussed.

Original languageEnglish (US)
Pages (from-to)235-256
Number of pages22
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume31
DOIs
StatePublished - 2002

Fingerprint

Protein folding
Protein Folding
Protein Stability
Proteins
Ligands
Deuterium
Thermodynamics
Hydrogen
Molecular Weight
Statistical mechanics
Macromolecules
Molecular weight
Nuclear magnetic resonance
Experiments

Keywords

  • Allosterism
  • Calorimetry
  • Cooperativity
  • Ligand binding
  • Protein stability
  • Thermodynamics

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology

Cite this

The linkage between protein folding and functional cooperativity : Two sides of the same coin? / Luque, Irene; Leavitt, Stephanie A.; Freire, Ernesto I.

In: Annual Review of Biophysics and Biomolecular Structure, Vol. 31, 2002, p. 235-256.

Research output: Contribution to journalArticle

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