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Left-handed topology of super-secondary structure formed by aligned α-helix and β-hairpin

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
302
Issue
1
Identifiers
DOI: 10.1016/0014-5793(92)80271-h
Keywords
  • α-Helix
  • β-Hairpin
  • Super-Secondary Structure
  • Amino Acid Sequence
  • Prediction
Disciplines
  • Biology
  • Design
  • Mathematics

Abstract

Abstract A novel super-secondary structure common for many non-homological proteins is considered. This folding pattern, consisting of adjacent along the chain α-helix and β-hairpin, has an aligned packing. It is found that one of the two possible ‘mirror-symmetrical’ topologies is observed in proteins. The α-helix + β-hairpin structures have a similar pattern of hydrophobic residues in their amino acid sequences. The remaining part of a molecule or a domain is almost always located on the same side of the considered folding pattern. These results can be used in the prediction of three-dimensional protein structure and protein design.

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