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Why are the same protein folds used to perform different functions?
A V Finkelstein1, A M Gutun, Badretdinov AYa
1Institute of Protein Research, Russian Academy of Sciences, Moscow Region.
FEBS Letters
|June 28, 1993
Summary
Popular protein folding patterns are thermodynamically stable, allowing stabilization by many random sequences. Rare folds require specific sequences, limiting their natural occurrence and functional diversity.
Area of Science:
- Biophysics
- Structural Biology
- Protein Science
Background:
- A limited set of protein folding patterns accounts for most known globular proteins.
- These common folds appear in non-homologous proteins with diverse functions.
Purpose of the Study:
- To investigate why certain protein folding patterns are prevalent in nature.
- To understand the relationship between sequence, structure, and function in proteins.
Main Methods:
- Analysis of protein folding patterns and their stability.
- Assessment of the number of random sequences that can stabilize different folds.
Main Results:
- 'Popular' protein folds possess thermodynamic advantages, enabling stabilization by numerous random sequences.
- Rarely observed folds are stabilized by very few random sequences.
- Prevalent folds are sequence-tolerant, facilitating diverse functional roles.
Conclusions:
- Thermodynamic stability is a key driver for the prevalence of specific protein folding patterns.
- Sequence tolerance in common folds allows for adaptation to various functions.
- Inherent structural 'weak points' in folding patterns may correlate with active site locations.