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Basic fibroblast growth factor is a beta-rich protein.

C S Wu1, S A Thompson, J T Yang

  • 1Cardiovascular Research Institute, University of California, San Francisco 94143-0524.

Journal of Protein Chemistry
|August 1, 1991
PubMed
Summary
This summary is machine-generated.

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Human basic fibroblast growth factor (bFGF) exhibits a predominantly beta-sheet structure, lacking alpha-helices. This protein undergoes an irreversible conformational change to a helix-like structure upon heating above 55°C.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Science

Background:

  • Human basic fibroblast growth factor (bFGF) is a key regulator of cell growth and differentiation.
  • Understanding the conformational dynamics of bFGF is crucial for elucidating its biological functions.

Purpose of the Study:

  • To investigate the secondary structure conformation of human basic fibroblast growth factor (bFGF).
  • To explore the conformational changes induced by environmental factors such as pH, temperature, and chemical agents.

Main Methods:

  • Circular dichroism (CD) spectroscopy was employed to analyze protein secondary structure.
  • Sequence prediction methods (Garnier et al.) were used for computational secondary structure analysis.
  • Analysis of CD spectra was performed using the Chang et al. least-squares method and the CONTIN program.

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Main Results:

  • Far-UV CD spectra indicated a predominantly beta-sheet structure with minimal to no alpha-helix content.
  • CD spectral analysis suggested approximately 50% beta-sheet composition, consistent with sequence predictions.
  • bFGF displayed an unusual CD band at 187 nm, sensitive to tyrosine ionization at pH 11.7.
  • Heating bFGF above 55°C induced an irreversible conversion to a helix-like conformation.
  • Helicity was also enhanced in the presence of trifluoroethanol and sodium dodecyl sulfate.
  • A mutant bFGF (Cys76Ser, Cys94Ser) exhibited similar conformational properties to the wild-type.

Conclusions:

  • Human bFGF possesses a largely disordered or beta-sheet-rich conformation in solution.
  • bFGF undergoes significant, irreversible thermal denaturation, transitioning to a helical structure.
  • The conformational stability and properties of bFGF are not critically dependent on its cysteine residues.