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Peptide: difference between revisions

Diff·revision 6 → 7·17:52, 2 Aug 2024

Difference between revision 6 and revision 7 of Peptide. 3 lines changed; the page grew by 375 bytes.

Revision 6 — 01:17, 23 Jul 2024
RotationRosalind (talk)
add the customs-detention point as a logistics fact, sourced
2,306 bytes ±0
Revision 7 — 17:52, 2 Aug 2024
TitrationTheo (talk)
rm the blanket claim that excursions are harmless
2,681 bytes +375
10Peptides are directional. By convention a sequence is written from the free amino terminus to the free carboxyl terminus, and the direction is not arbitrary: the same residues in reverse order are a different molecule with different properties. This is the reason a sequence given without its direction is ambiguous.{{r|iupac}}10Peptides are directional. By convention a sequence is written from the free amino terminus to the free carboxyl terminus, and the direction is not arbitrary: the same residues in reverse order are a different molecule with different properties. This is the reason a sequence given without its direction is ambiguous.{{r|iupac}}
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+12Almost everything else on this wiki is a peptide or is about peptides — their [[Peptide synthesis|synthesis]], their [[Analytical method validation|analysis]], their [[Cold chain|handling]] and their supply. Peptides sold for laboratory research are not approved for human use, whatever their sequence resembles; see [[Research use only]].
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12== Structure ==14== Structure ==
13The amide bond has partial double-bond character, which restricts rotation and makes the six atoms of the peptide unit approximately planar. Conformational freedom therefore resides in the two dihedral angles either side of each α-carbon, and it is the accessible combinations of these that give rise to the α-helix, the β-sheet and the turn.{{r|iupac}}15The amide bond has partial double-bond character, which restricts rotation and makes the six atoms of the peptide unit approximately planar. Conformational freedom therefore resides in the two dihedral angles either side of each α-carbon, and it is the accessible combinations of these that give rise to the α-helix, the β-sheet and the turn.{{r|iupac}}
24[[Category:Compounds and pharmacology]]26[[Category:Compounds and pharmacology]]
25[[Category:Peptide synthesis]]27[[Category:Peptide synthesis]]
+28[[Category:Analytical science]]
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