Sandbox Reserved 966: Difference between revisions
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The light chain of '' Clostridium botulinum '' neurotoxin serotype A presents several typical structures. | The light chain of '' Clostridium botulinum '' neurotoxin serotype A presents several typical structures. | ||
*The polypeptide forms 11 α-helices (we can notice a kink formed by <scene name='60/604485/Thr101/1'>Thr101</scene>, who may interact with an H from the N of Gly104) | *The polypeptide forms 11 α-helices (we can notice a kink formed by <scene name='60/604485/Thr101/1'>Thr101</scene>, who may interact with an H from the N of Gly104) | ||
*We can also find tree 3-10 helices | *We can also find tree 3-10 helices (<scene name='60/604485/H3/2'>H3</scene>, <scene name='60/604485/H13/1'>H13</scene>, <scene name='60/604485/H14/1'>H14</scene>) | ||
*There are several <scene name='60/604485/Sheets/1'>β sheets </scene> that are anti parallel except <scene name='60/604485/Sheets_parrallel/1'>this one.</scene> | *There are several <scene name='60/604485/Sheets/1'>β sheets </scene> that are anti parallel except <scene name='60/604485/Sheets_parrallel/1'>this one.</scene> | ||
* An interesting structure is also a typical <scene name='60/604485/Betaturn/1'>β-turn</scene> : indeed the chain makes a sharp reversal by 180° within 4 residues, moreover Cα from the ''i'' residue and the Cα from the ''i+3'' residue are separated by less than 7 angstroms. | * An interesting structure is also a typical <scene name='60/604485/Betaturn/1'>β-turn</scene> : indeed the chain makes a sharp reversal by 180° within 4 residues, moreover Cα from the ''i'' residue and the Cα from the ''i+3'' residue are separated by less than 7 angstroms. | ||
