FAQs
Technical
- What are pseudoproline amino acids and what advantage do they have in peptide synthesis?
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What are the typical contaminants associated with peptide synthesis?
For purified peptides, the main contaminants are deletions and truncations of the parent sequence. This occurs when the reaction efficiency of the incoming amino acid is reduced due to factors such as steric hindrance and secondary structure of the growing peptide chain. A truncation is a C-terminal fragment of the peptide which is shorter than the parent. A deletion is the parent sequence which I missing one or more amino acids in any part of the peptide. Certain reagents which are used in the work up to cleave the peptide from the solid phase may also carry over, however, these are volatile and evaporated in the freeze-drying process and removed during the purification step.
- 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?