Loop fold structure of proteins: resolution of Levinthas paradox
Related Experiment Video
Updated: Sep 30, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Igor N Berezovsky1, Edward N Trifonov
1Department of Structural Biology, The Weizmann Institute of Science, P.O.B. 26, Rehovot 76100, Israel. Igor.Berezovsky@weizmann.ac.il
Abstract:
According to Levinthal a protein chain of ordinary size would require enormous time to sort its conformational states before the final fold is reached. Experimentally observed time of folding suggests an estimate of the chain length for which the time would be sufficient. This estimate by order of magnitude fits to experimentally observed universal closed loop elements of globular proteins - 25-30 residues.
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein and Protein Structure
Protein Organization
Protein Organization
The primary structure of a protein is its amino acid sequence.

