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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Recent mechanistic insights into conformational interconversion in metamorphic proteins.

Buyuan Ma1, Sainan Li2, Zengxin Ma3

  • 1College of Life Sciences, Qingdao Agricultural University, Qingdao, 266109, China; Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China.

International Journal of Biological Macromolecules
|January 3, 2026
PubMed
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Metamorphic proteins can adopt multiple distinct native folds, enabling dynamic regulation of function. This review explores the mechanisms and principles behind this fold-switching behavior.

Keywords:
Fold-switchingMetamorphic proteinsNMR

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Metamorphic proteins challenge the classical Anfinsen paradigm by exhibiting multiple distinct native folds.
  • These proteins reversibly interconvert between folds under physiological conditions, often regulated by environmental cues.
  • This fold-switching allows for dynamic control over protein function and adaptation.

Purpose of the Study:

  • To review recent mechanistic insights into six well-characterized metamorphic proteins.
  • To discuss the structural, thermodynamic, and kinetic principles governing protein fold-switching.
  • To highlight the role of advanced NMR techniques in studying these dynamic processes.

Main Methods:

  • Review of existing literature on metamorphic proteins.
  • Analysis of structural, thermodynamic, and kinetic data.
  • Emphasis on advanced Nuclear Magnetic Resonance (NMR) techniques.

Main Results:

  • Detailed mechanistic insights into KaiB, RfaH, XCL1, ORF9b, GX A/GX B, and Sa1V90T.
  • Identification of environmental cues regulating fold-switching.
  • Quantification of interconversion rates and mapping of conformational landscapes.

Conclusions:

  • Protein fold-switching is a regulated adaptive mechanism.
  • Advanced NMR techniques are crucial for atomic-resolution studies of protein dynamics.
  • A comprehensive framework for understanding metamorphic proteins is emerging.