A thermodynamic analysis of fibrillar polymorphism

Martin D Jeppesen, Kim Hein, Poul Nissen, Peter Westh, Daniel E Otzen

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Abstract

We explore the thermodynamic properties of three different fibrils of the peptide hormone glucagon, formed under different salt conditions (glycine, sulfate and NaCl, respectively), and differing considerably in compactness. The three fibrils display a large variation in the specific heat capacity DeltaC(p) determined by isothermal titration calorimetry. Sulfate fibrils show a negative DeltaC(p) expected from a folding reaction, while the DeltaC(p) for glycine fibrils is essentially zero. NaCl fibrils, which are less stable than the other fibrils, have a large and positive C(p). The predicted change in solvent accessible area is not a useful predictor of fibrillar DeltaC(p) unlike the case for globular proteins. We speculate that strong backbone interactions may lead to the unfavorable burial of polar side residues, water and/or charged groups which all can have major influence on the change in C(p). These results highlight differences in the driving forces of native folding and fibril formation.
Original languageEnglish
Book seriesAdvances in Biophysical Chemistry
Volume149
Issue1-2
Pages (from-to)40-6
Number of pages7
ISSN1057-8943
DOIs
Publication statusPublished - 1 Jun 2010

Keywords

  • Amino Acid Sequence
  • Calorimetry
  • Circular Dichroism
  • Glucagon
  • Glycine
  • Molecular Sequence Data
  • Pancreatic Elastase
  • Protein Folding
  • Protein Structure, Tertiary
  • Sodium Chloride
  • Sulfates
  • Thermodynamics

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