The protonated form of orthanilic acid may interact with the charged amino acid residues in peptides. For example, it can form hydrogen bonds with the negatively charged carboxyl groups of aspartic acid and glutamic acid. These interactions can potentially influence the folding of peptides by stabilizing or destabilizing specific conformations.
If you need to purchase chemical raw materials, submit your demand information to get the latest quotations.
methyl ((2-(2-(2-((tert-butoxycarbonyl)amino)-4-methylpentanamido)-2-methylpropanamido)phenyl)sulfonyl)-L-prolinate
2’-O-(4,4’-dimethoxytrityl)-4’-C-(azidomethyl)-5’-azido-5’-deoxyuridine
3-(acetoxymethyl)-6-methyl-N-(acetyl)aniline
N-[2-[3-benzoyl-4-[(4-methylphenyl)acetylamino]phenyl]]-Nγ-tert-butyloxycarbonyl-γ-aminobutyric acid amide
2,9-bis[p-(formyl)phenyl]-1,10-phenanthroline
5,6-oxido-3β,20β-dihydroxypregnane dibenzoate
