Role of Hydrophobic Interactions in Protein Chain Folding during Biosynthesis

A. V. Trikulenko

Lviv Franko State University, ul. Grushevskogo 4, Lviv, 290005 Ukraine; fax: (0322) 27-1668

Received September 22, 1997; Revision received December 23, 1997

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It has been found that hydrophobic potentials of 30- to 40-amino acid fragments of amino acid sequences of myoglobin, cytochrome b₅, alpha-chymotrypsin, and seven other globular proteins analyzed are similar and correspond to free energies of formation of limited hydrophobic nuclei.

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KEY WORDS: hydrophobic nuclei, hydrophobic potentials, hydrophobic interactions, protein chain folding

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