TERTIARY STRUCTURES OF GASTRIN‐LIKE TETRAPEPTIDES

Tsutoo Yamada; Hiroshi Wako; Nobuhiko Saitô; Yoshinori Isogai; Hiroshi Watari

doi:10.1111/j.1399-3011.1976.tb02541.x

TERTIARY STRUCTURES OF GASTRIN‐LIKE TETRAPEPTIDES

Tsutoo Yamada, Hiroshi Wako, Nobuhiko Saitô^*, Yoshinori Isogai, Hiroshi Watari

^*Corresponding author for this work

School of Social Sciences

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

Tertiary structures of gastrin‐like tetrapeptide Trp‐Met‐Asp‐Phe‐NH₂ and those substituted by Leu, Val or Gly for Met are studied. The lowest energy conformations of the side chains when the back bone is fixed in α‐helix are obtained by modified minimization algorithm. It is suggested that protein folding proceeds in the accessible conformation space as a self‐organization process leading to minimum energy conformation in this space.

Original language	English
Pages (from-to)	607-614
Number of pages	8
Journal	International Journal of Peptide and Protein Research
Volume	8
Issue number	6
DOIs	https://doi.org/10.1111/j.1399-3011.1976.tb02541.x
Publication status	Published - 1976 Nov

ASJC Scopus subject areas

Biochemistry

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abstract = "Tertiary structures of gastrin‐like tetrapeptide Trp‐Met‐Asp‐Phe‐NH2 and those substituted by Leu, Val or Gly for Met are studied. The lowest energy conformations of the side chains when the back bone is fixed in α‐helix are obtained by modified minimization algorithm. It is suggested that protein folding proceeds in the accessible conformation space as a self‐organization process leading to minimum energy conformation in this space.",

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AU - Yamada, Tsutoo

AU - Wako, Hiroshi

AU - Saitô, Nobuhiko

AU - Isogai, Yoshinori

AU - Watari, Hiroshi

PY - 1976/11

Y1 - 1976/11

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AB - Tertiary structures of gastrin‐like tetrapeptide Trp‐Met‐Asp‐Phe‐NH2 and those substituted by Leu, Val or Gly for Met are studied. The lowest energy conformations of the side chains when the back bone is fixed in α‐helix are obtained by modified minimization algorithm. It is suggested that protein folding proceeds in the accessible conformation space as a self‐organization process leading to minimum energy conformation in this space.

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TERTIARY STRUCTURES OF GASTRIN‐LIKE TETRAPEPTIDES

Abstract

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