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Related Experiment Videos

In vitro evolution of thermodynamically stable turns

H X Zhou1, R H Hoess, W F DeGrado

  • 1DuPont Merck Pharmaceutical Company, Wilmington, Delaware 19880-0336, USA.

Nature Structural Biology
|May 1, 1996
PubMed
Summary
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Protein primary structure influences turn formation. Stable protein structures favor specific turn sequences, indicating evolutionary pressure for thermodynamic stability in beta-turns.

Area of Science:

  • Protein structure and stability
  • Molecular biology
  • Biophysics

Background:

  • Protein primary structure dictates higher-order structures.
  • Beta-turns are crucial for protein folding and function.
  • The role of primary sequence in turn formation is not fully understood.

Purpose of the Study:

  • To investigate how primary structure dictates beta-turn formation.
  • To assess the impact of host protein stability on turn sequence selection.
  • To determine if evolutionary pressure favors thermodynamically stable turn structures.

Main Methods:

  • Substitution of native turn sequences with random sequences in host proteins.
  • Measurement of active protein fraction as a function of host stability and temperature.

Related Experiment Videos

  • Thermodynamic analysis of selected turn sequences.

    • Main Results:

    • Highly stable host proteins accommodated a higher fraction of functional random turn sequences.
    • Decreasing host stability and increasing temperature reduced the fraction of supporting sequences.
    • Selected turn sequences often resembled wild-type or known turn preferences.
    • Sequences selected under stringent conditions yielded the most stable proteins.

    Conclusions:

    • Primary structure plays a significant role in specifying protein turns.
    • Beta-turns are under evolutionary selection for thermodynamic stability.
    • Protein stability is a key factor in the success of sequence variations in turns.