Structure of residues 1540 in antiparallel D23NAβ 140 (SFg2
Beta Sheet Antiparallel. Antiparallel ß sheets are slightly more. Web the side chains in the beta sheet are normal to the plane of the sheet, extending out from the plane on alternating sides.
Structure of residues 1540 in antiparallel D23NAβ 140 (SFg2
Web the side chains in the beta sheet are normal to the plane of the sheet, extending out from the plane on alternating sides. Parallel sheets characteristically distribute hydrophobic side chains on both. This can occur in the presence of two consecutive proline residues, which create an angled kink in. Antiparallel ß sheets are slightly more.
Parallel sheets characteristically distribute hydrophobic side chains on both. Web the side chains in the beta sheet are normal to the plane of the sheet, extending out from the plane on alternating sides. This can occur in the presence of two consecutive proline residues, which create an angled kink in. Parallel sheets characteristically distribute hydrophobic side chains on both. Antiparallel ß sheets are slightly more.
