A Perspective on the (Rise and Fall of) Protein β-Turns

Int J Mol Sci. 2022 Oct 14;23(20):12314. doi: 10.3390/ijms232012314.

Abstract

The β-turn is the third defined secondary structure after the α-helix and the β-sheet. The β-turns were described more than 50 years ago and account for more than 20% of protein residues. Nonetheless, they are often overlooked or even misunderstood. This poor knowledge of these local protein conformations is due to various factors, causes that I discuss here. For example, confusion still exists about the assignment of these local protein structures, their overlaps with other structures, the potential absence of a stabilizing hydrogen bond, the numerous types of β-turns and the software's difficulty in assigning or visualizing them. I also propose some ideas to potentially/partially remedy this and present why β-turns can still be helpful, even in the AlphaFold 2 era.

Keywords: AlphaFold 2; DSSP; bend; hydrogen bonds; secondary structure; secondary structure assignment method; sequence structure relationship.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Hydrogen Bonding
  • Protein Conformation
  • Protein Structure, Secondary
  • Proteins* / chemistry

Substances

  • Proteins