4

Protein sequencing is a nicely constrained problem: you have a one-dimensional sequence of amino acid members, which come from a limited set of options (made a bit more complicated by post-translational modifications, but not much more so). Because it's one-dimensional, it's a problem you can easily solve by chopping up a protein into little bits, using mass ...


4

As their name suggests, the majority of a ribosome's structure and function come from ribonucleic acid (RNA), not protein. While ribosomes are about 35%-40% protein on average, a majority of ribosomal proteins are not essential for the catalytic functions of the ribosome, and none are in direct contact with the catalytic reaction site where peptide bonds are ...


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".


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

To answer why sequences are known before structures, it is worth highlighting the typical ‘workflow’ for a biochemical researcher. Briefly, sequence is always before structure because you need the sequence to determine the structure. As with everything else one would like to investigate, you have to start with the information that you already have. In modern ...


2

There's a Wikinome page called Phosphorylation of unusual amino acids describing phosphorylation of histidine, aspartate, cysteine, lysine, and arginine. Lysine and arginine are apparently phosphorylated on the nitrogens. I was a little surprised to see histidine and aspartate on the list, as histidine kinases seem to come up often in my area of research. I'...


2

Good question, this regards rotamers! Basically, the side chain of amino acids can rotate as shown in the figure below for glutamate (Glu; E). The various option for side-chain rotation is called rotamers! Some amino-acids side chains have the potential of many rotamers (such as glutamate) while some can only adopt a few (such as tryptophan) due to steric ...


1

On our planet, there is such an incredibly massive amount of protein creation by biological organisms (as well as smaller peptide constructs) that it would be essentially impossible to identify any that was created by a natural non-biological process. Moreover, now that there is life, any location with the right conditions for non-biological creation of ...


1

There are research groups working on this exact question; understanding cold adaptation in enzymes. You can read about this in several articles such as 'Computation of enzyme cold adaptation', or 'Molecular Structural Basis for the Cold Adaptedness of the Psychrophilic β-Glucosidase BglU in Micrococcus antarcticus', or 'Specific amino acids responsible for ...


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