Structure and stability of the alpha-helix: lessons for design.
The alpha-helix is the most abundant secondary structure in proteins. We now have an excellent understanding of the rules for helix formation because of experimental studies of helices in isolated peptides and within proteins, examination of helices in crystal structures, computer modeling and simulations, and theoretical work. Here we discuss structural features that are important for designing peptide helices, including amino acid preferences for interior and terminal positions, side chain interactions, disulfide bonding, metal binding, and phosphorylation. The solubility and stability of a potential design can be predicted with helical wheels and helix/coil theory, respectively. The helical content of a peptide is most often quantified by circular dichroism, so its use is discussed in detail.
Errington
Neil
N
The University of Manchester, Manchester, UK.
Iqbalsyah
Teuku
T
Doig
Andrew J
AJ
D002942:Circular Dichroism; D004220:Disulfides / Q000737:chemistry; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary / Q000235:genetics; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D004220:Disulfides; D008670:Metals; D010455:Peptides; D011506:Proteins