FAQs
Technical
-
What are pseudoproline amino acids and what advantage do they have in peptide synthesis?
Pseudoproline dipeptide reagents are special secondary structure disrupting amino acid reagents based on serine and threonine. They stop the peptide forming secondary structure whilst the peptide is growing on the solid phase. This is thought to be one of the main issues with successful peptide synthesis. On cleavage the native sequence is re-established.
- What are the typical contaminants associated with peptide synthesis?
- What is the difference between peptide purity and peptide yield?
- What are the typical salts associated with my peptide?
- If I have biotin in my peptide, do I need a spacer between the biotin group and the peptide sequence and if so which spacer should I use?
- What can I do to increase the cell permeability of a peptide?
- How do I solubilize my peptides?
- How do I characterize batches of my "drug candidate" peptide, which contains a D-amino acid?
- How do you calculate hydrophobicity?