4

There are two main methods for discerning a protein's structure; x-ray crystallography, and more recently cryo-electron microscopy. Both methods work by firing a high-energy beam through the sample and observing how the path of the beam has been changed by passing through the sample. The data obtained by measuring the beam includes "signal" ...


3

The lipoprotein has a 36 amino acid sequence that is the same (matches) as part of a protein from SARS-Cov-2. The newspaper article refers to this paper below. "Intranasal fusion inhibitory lipopeptide prevents direct contact SARS- CoV-2 transmission in ferrets" Rory D. de Vries1@, Katharina S. Schmitz1@, Francesca T. Bovier#2,3,4@, Danny Noack1, ...


3

Yes, stretch means sequence in this context. See definition #5 for stretch (noun) on Wiktionary: A segment or length of material. So, the "stretch of amino acids" in the article refers to the peptide sequence portion of the lipopeptide prophylactic.


3

Yes, it was solved in the early 1960s, starting about 1961. See Wikipedia's Genetic Code - History, and perhaps "Establishing the Triplet Nature of the Genetic Code".


1

I have found this image on Biology LibreTexts, and they have answered my question. Like I suspected, the large residues will mainly project out of the beta pleated sheet and will not interfere much with the backbone hydrogen bonds. In alpha helices, however, the branched and aromatic residues are still able to project into the helix (as they are not pointing ...


1

This table is from the Wikipedia page for α-helix: As you can see aromatics are not the worst offenders. In fact, barring proline (whose backbone torsion angles are unsuited to helices), Gly is the worst offender. A likely reason for this is Gly being too flexible i.e. its small side chain H allows it to adopt backbone torsion angles unsuited for α-helix. ...


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