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

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 conform...

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Bibliographic Details
Published in:International journal of molecular sciences 2022-10, Vol.23 (20), p.12314
Main Author: de Brevern, Alexandre G
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
bend
DSSP
Hydrogen Bonding
Hydrogen bonds
Polypeptides
Protein Conformation
Protein structure
Protein Structure, Secondary
Proteins
Proteins - chemistry
Review
Secondary structure
secondary structure assignment method
sequence structure relationship
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Summary: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.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms232012314