Liquid syntax error (snippets/seo-jsonld line 46): Variable '{{ shop.url | append: routes.search_url | append: '?q={search_term_string}' was not properly terminated with regexp: /\}\}/ Skip to content

Free Express shipping over $300 · Ships from CanadaFree Express over $300

Horizon® Peptides

Quiz · peptide basics

Research quiz

Twelve questions on what peptides are, how they are written and how they are made. Each answer comes with an explanation and the guide that covers it.

Question 1 of 12

  1. 1. What joins one amino acid to the next in a peptide?

    Show the answer

    Answer A peptide bond: an amide link formed with the loss of one water molecule

    A peptide bond forms when the carboxyl group of one amino acid reacts with the amino group of the next, releasing a molecule of water. The result is an amide link, and a chain of them is the backbone of every peptide and protein. Disulfide bridges and hydrogen bonds shape a chain once it exists; they are not what holds its residues in order.

    Read the guide: What Are Peptides?

  2. 2. What mainly separates the words peptide and protein?

    Show the answer

    Answer The length of the chain

    Peptides and proteins are built from the same amino acids, joined by the same peptide bonds. The words differ by size: a short chain is called a peptide, and a long, folded one a protein. The line between them is a convention rather than a law of chemistry, and it is usually drawn at around fifty residues.

    Read the guide: Peptide vs Protein vs Amino Acid

  3. 3. A sequence is written from left to right. Which end of the chain comes first?

    Show the answer

    Answer The N-terminus, with its free amino group

    By convention a peptide sequence is written from the N-terminus, the end with a free amino group, to the C-terminus, the end with a free carboxyl group. The convention matters because a chain read backwards is a different molecule: the same residues in the opposite order do not have the same chemistry.

    Read the guide: Peptide Nomenclature and Modifications

  4. 4. How many amino acids does the standard genetic code specify?

    Show the answer

    Answer 20

    The standard genetic code specifies twenty amino acids, each with a three-letter and a one-letter abbreviation. Sixty-four is the number of three-base codons, several of which stand for the same amino acid. A synthetic peptide can also carry building blocks from outside the twenty, such as D-amino acids or Aib, because a chemist is not limited to what a ribosome can use.

    Read the guide: What Are Peptides?

  5. 5. What does lyophilization remove from a peptide?

    Show the answer

    Answer Water

    Lyophilization, or freeze-drying, freezes a solution and then lowers the pressure so that the ice turns directly into vapour. What is left is a dry solid. Water is removed because most of the reactions that degrade a peptide need it. Counter-ions, and any impurities present before drying, stay in the dried material.

    Read the guide: Why Peptides Are Lyophilized

  6. 6. What does Ac- at the start of a written sequence mean?

    Show the answer

    Answer The N-terminus carries an acetyl group

    Ac- is shorthand for an acetyl group attached to the amino group at the N-terminus, a modification called N-terminal acetylation. It removes the positive charge that end of the chain would otherwise carry and adds about 42 daltons to the mass. It has nothing to do with an acetate salt, in which acetate is a separate counter-ion and not part of the peptide.

    Read the guide: Peptide Nomenclature and Modifications

  7. 7. What does -NH2 at the end of a written sequence mean?

    Show the answer

    Answer The C-terminus is an amide instead of a free acid

    A sequence that ends in -NH2 has a C-terminal amide: the carboxyl group at the end of the chain has been converted to a carboxamide. Amidation removes the negative charge a free acid would carry at neutral pH, and it lowers the mass by about one dalton compared with the free acid.

    Read the guide: Peptide Nomenclature and Modifications

  8. 8. How does a D-amino acid differ from its L-form?

    Show the answer

    Answer It is the mirror image: the same atoms with the opposite handedness

    D- and L-amino acids are mirror images of each other, like a left and a right hand. They share a formula, a mass and a side chain, and differ only in the arrangement of groups around the alpha carbon. Ribosomes build proteins from L-amino acids. Chemists place D-residues in synthetic peptides because the enzymes that cut peptide chains are, for the most part, specific to the L-form.

    Read the guide: Peptide Nomenclature and Modifications

  9. 9. How are most research peptides manufactured?

    Show the answer

    Answer By solid-phase synthesis: one residue at a time, on a chain anchored to resin beads

    Most research peptides are made by solid-phase peptide synthesis. The first amino acid is anchored to an insoluble resin and the chain grows one protected residue at a time, with washing between the steps. At the end the chain is cleaved from the resin and purified. No coupling step is perfectly complete, and that is where most synthesis-related impurities come from.

    Read the guide: Solid-Phase Peptide Synthesis

  10. 10. A finding is reported from an experiment in cultured cells. Which statement is correct?

    Show the answer

    Answer It shows what happened in that cell system, under those conditions

    Cell-culture work is the first rung of the evidence ladder. It can show that a compound binds a receptor, or changes what a cell does, under controlled conditions. It cannot show what happens in a whole organism, where absorption, distribution, metabolism and many interacting tissues come into play. Animal studies and controlled clinical trials are separate, higher levels of evidence, and a finding at one level does not carry over to the next by itself.

    Read the guide: Evidence Levels in Peptide Research

  11. 11. What is a disulfide bridge?

    Show the answer

    Answer A covalent bond between the sulfur atoms of two cysteine residues

    A disulfide bridge is a covalent bond between the sulfur atoms of two cysteine side chains. It can link two parts of one chain, closing a loop, or join two separate chains. Oxytocin is an example: a nine-residue peptide whose two cysteines are joined in this way. Methionine also contains sulfur, but it cannot form the bridge.

    Read the guide: Peptide Glossary

  12. 12. Which of these is a chemical route by which a peptide degrades?

    Show the answer

    Answer Oxidation of a methionine side chain

    Oxidation is one of the common chemical routes of peptide degradation: methionine, and to a lesser extent cysteine and tryptophan, react with oxygen. The other main routes are deamidation of asparagine and glutamine, hydrolysis of the backbone, and aggregation. Water, heat, light and oxygen speed them up, which is why peptides are kept dry, cold and in the dark.

    Read the guide: Peptide Stability and Degradation

How this works

A short check of what you know, built to teach as it goes.

  1. One question at a time

    Choose an answer and you see at once whether it was right, with a paragraph on why. There is no timer and no trick wording.

  2. Settled science only

    Every question has one textbook answer: bonds, units, methods. Nothing here is about what a compound does, and nothing is medical.

  3. A reading list at the end

    The result lists the guides behind the questions you missed first. No sign-up is asked for and your answers are not stored.

More research tools

This quiz covers research peptides as laboratory chemistry. It contains no dosing information and no guidance on use in people or animals.