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The design of water soluble β-sheet structure based on a nucleation strategy

✍ Scribed by Humberto Díaz; Kwok Yin Tsang; Danny Choo; Jeffery W. Kelly

Publisher
Elsevier Science
Year
1993
Tongue
French
Weight
968 KB
Volume
49
Category
Article
ISSN
0040-4020

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✦ Synopsis

This manuscript demonstrates that incorporation of the amino acid residue 4-(2-aminoethyl)-6-dibenzofuranpropionic acid 1 is necessary but not sufficient to stabilize the &sheet structure of a heptapeptide in water. A sequence which facilitates intrastrand hydrophobic interactions is also bqortant.

Introduction. gsheet secondary structure is as common as a-helical structure in proteins, but unlike the H. DIAZ et al.

Polypeptides fold when the AS* term is greater in magnitude than the A&a term ( Equation 1). In the denatured state the Sm term is unfavorable relative to the folded state due to the ordexxi hydration shells required to solvate the hydrophobic side chains. As the peptide. chain folds, the SW-term incmases due to the ordered water liberated from the interacting hydrophobic groups. Releasing ordered water overcomes the unfavorable entropy term associated with restricting the conformation of the chain which occurs during secondary structure formation. A. Ideally. Intmmoledar Folding Rccceds Selfhsociiott Affording a Ho~nOttS ~-Sheet SrmCture B. Gften FMittg and Self-Association Have Comparable Rates Which Leads to a Heterogeneous BSheet FIGURE 1.

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