Overview

beta-type structures


Related Overviews

 

'beta-type structures' can also refer to...

 

More Like This

Show all results sharing this subject:

  • Medicine and Health

GO

Show Summary Details

Quick Reference

Various secondary structural regions of proteins formed from beta-strands (as opposed to alpha-helical regions). Beta-strands are stretches of amino acids (5–10 aa) in which the peptide backbone is almost fully extended. Beta-arches involve two adjacent antiparallel beta-strands from different sheets, joined by a coiled region usually forming a beta-sandwich. In beta-barrels a series of (typically amphipathic) beta sheets are arranged around a central pore as in voltage-gated ion channels. Beta hairpins are antiparallel beta strands lying adjacent in a sheet. A beta-helix is a large right-handed coil (or superhelix) containing two or three beta-sheets. Beta pleated sheets (beta-sheets) are formed from multiple strands—parallel, antiparallel, or a mixture—linked by interchain hydrogen bonds between peptide carboxyl and amino groups.

Subjects: Medicine and Health.


Reference entries

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.