Introducing the Levinthal's Protein Folding Paradox and Its Solution

Author(s)

Martinez, Leandro ^[1]

Affiliation

^[1] Univ Estadual Campinas, Inst Chem, Dept Phys Chem, BR-13083970 Sao Paulo - Brazil

• Document type: Journal article
• Source: Journal of Chemical Education; v. 91, n. 11, p. 1918-1923, NOV 2014.
• Web of Science Citations: 4

Abstract

The protein folding (Levinthal's) paradox states that it would not be possible in a physically meaningful time to a protein to reach the native (functional) conformation by a random search of the enormously large number of possible structures. This paradox has been solved: it was shown that small biases toward the native conformation result in realistic folding times of realistic-length sequences. This solution of the paradox is, however, not amenable to most chemistry or biology students due to the demanding mathematics. Here, a simplification of the study of the paradox and its solution is provided so that it is accessible to chemists and biologists at an undergraduate or graduate level. Despite its simplicity, the model captures some fundamental aspects of the protein folding mechanism and allows students to grasp the actual significance of the popular folding funnel representation of the protein energy landscape. The analysis of the folding model provides a rich basis for a discussion of the relationships between kinetics and thermodynamics on a fundamental level and on student perception of the time-scales of molecular phenomena. (AU)

• FAPESP's process: 13/05475-7 - Computational methods in optimization
• Grantee: Sandra Augusta Santos
• Support Opportunities: Research Projects - Thematic Grants
• FAPESP's process: 10/16947-9 - Correlations between dynamics, structure and function in protein: computer simulations and algorithms
• Grantee: Leandro Martinez
• Support Opportunities: Regular Research Grants