摘要
This article is concerned with the so-called Levinthal’s paradox. It will be argued that many have sought a “solution” to Levinthal’s paradox, where in fact, the “solution” already appeared in Levinthal’s original articles. Most of the subsequent suggested “solutions” were inadequate solutions to a non-paradox. It is shown that the discovery of strong hydrophilic forces not only dismisses the Levintal paradox, but also provides a solution to the general problem of protein folding. A simple model based on the Markov process is presented to demonstrate how a strong biased-force can dramatically reduce the number of steps required to reach the stable native 3-D structure of the protein.
This article is concerned with the so-called Levinthal’s paradox. It will be argued that many have sought a “solution” to Levinthal’s paradox, where in fact, the “solution” already appeared in Levinthal’s original articles. Most of the subsequent suggested “solutions” were inadequate solutions to a non-paradox. It is shown that the discovery of strong hydrophilic forces not only dismisses the Levintal paradox, but also provides a solution to the general problem of protein folding. A simple model based on the Markov process is presented to demonstrate how a strong biased-force can dramatically reduce the number of steps required to reach the stable native 3-D structure of the protein.
