Science Links Japan | Theoretical Conformational Analysis of .ALPHA.-Hairpin Structures of Polypeptides. [40]. Stabilization of .ALPHA.-Hairpin Structures by Disulfide-Bond Formation at the Middle Portion of Helices.

Theoretical Conformational Analysis of .ALPHA.-Hairpin Structures of Polypeptides. [40]. Stabilization of .ALPHA.-Hairpin Structures by Disulfide-Bond Formation at the Middle Portion of Helices.

Accession number;99A0228211

Title;Theoretical Conformational Analysis of .ALPHA.-Hairpin Structures of Polypeptides. [40]. Stabilization of .ALPHA.-Hairpin Structures by Disulfide-Bond Formation at the Middle Portion of Helices.

Author; OKA MASAHITO (Univ. of Osaka Prefect.) HAYASHI TOSHIO (Univ. of Osaka Prefect.) ISHIKAWA YUICHIRO (Osaka Inst. of Technol.) HIRANO YOSHIAKI (Osaka Inst. of Technol.)

Journal Title;Abstracts. Symposium on Biofunctional Chemistry

Journal Code:L0836A

ISSN:

VOL.13th;NO.;PAGE.67-69(1998)

Figure&Table&Reference;

Pub. Country;Japan

Language;Japanese

Abstract;We tried to introduce the disulfide linkage at the end portion of the helices for stabilizing the .ALPHA.-hairpin structure, and it is theoretically investigated how such disulfide-bond formation effects on the packing motif of two .ALPHA.-helices in .ALPHA.-hairpin structures. Calculated results indicate that it is possible to introduce the disulfide linkage at the N- and C-terminal portions of polypeptides for stabilizing the .ALPHA.-hairpin structure. And their adequate positions for introducing a disulfide linkage can be theoretically predicted from the results of theoretical analysis using the Ala residue approximation. (author abst.)

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