Tag Info

New answers tagged

0

In vitro translation is not as efficient as other chemical polymer reactions. For example, when proteins are synthesized using in vitro translation systems, many researchers have been using radio-labeling to see the products because the yield is too low to detect them by other methods, although few small proteins have been successfully produced at a ...


3

A protein-protein interaction (PPI) binding site is a type of interface. If it has been established that the interface is a PPI binding site, then the terms can from that point forward be used interchangeably. But the word "interface" is very generic and does not have any specific scientific meaning so the nature of the interface must be defined or else the ...


0

By "still work" I assume you are asking if it will still be recognized by an antibody? It might. Internal T7 tag fusions are done, though they may require different antibodies than terminally tagged fusions. That said, do you have a reason for inserting the the tag after methionine? The T7 tag already starts with methionine and naturally functions to ...


-1

You need a ribosomal binding site before the initial codon.


1

It will depend on the drug you are using. There is a pathway that forms the translational initiation complex that starts with binding the mRNA's cap, the small subunit scans to find the AUG, then the large subunit binds, and so on. The 80 S peaks on the density gradients are not vacant, they are poised on mRNAs waiting to initiate (if you removed the ...


5

Shimadzu explains peptide mapping as follows: Peptide mapping involves selectively cleaving the individual target [proteins] using an appropriate enzyme or chemical and analyzing the peptide fragments obtained using HPLC [high-performance liquid chromatography] or another suitable method. [... I]dentification of the peptide fragments separated by LC ...


10

Overview Modelling has come on leaps and bounds over the last decade or so and in many cases has acted as a sometimes viable, and inexpensive substitute for experimental structures. How do you know when you get it right? Ultimately, one still needs experimental evidence to know when a model generated in silico is right. But there are ways of scoring ...


0

At this point, it must be verified experimentally. In this foldit research paper, they use software and user input to design essentially an enhanced version of a naturally occurring protein, but they then physically make their new protein and determine its structure experimentally, using x-ray crystallography. Overall, they use a lot of trial and error ...


0

IMO, this is by far the best introduction to enzyme mechanisms and protein folding, by a leading researcher in the field. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding by Alan Fersht


4

Short answer: there are no restrictions in principle on which amino acids can follow which. That means that in principle you can have polypeptide in any configuration: AAAA, WQWQWQ etc. Problem is that polypeptides must be functional and, because they are in aqueous solution, it puts restrictions on how polypeptide form secondary and tertiary structure. It ...


0

To answer your question: No, there are no restrictions to what amino acid is next ("a nearest neighbor") to its N-terminal or C-terminal neighbor.


0

Are you sure that the RSA formula is right? I have found a different description:Relative solvent accessibility classes are usually derived from the DSSP program by normalizing it at the maximum value of exposed surface area obtainable for each residue.Different arbitrary threshold values of solvent accessibility are chosen to define binary categories ...


6

Have a look at this paper. They have isolated a chromoprotein similar to GFP, and like the latter it does not have any prosthetic group. This protein — asFP595 (because it was isolated from the anemone Anemonia sulcata.), is purple coloured under white light and also exhibits a little fluorescent emission in the red region (λmax = 595 nm). Also have a ...


1

You are looking for light-emitting proteins. They gather energy from either absorption of photon (fluorescence) or via random thermal fluctuations. Problem is that fluorescence might be considered forced emission, whereas what you looking for is results of spontaneous transitions. That means that number of photons per second you can expect from latter ...


0

That depends on what your are trying to do. Apparently your query sequence is similar to that of proteins with a known 3D-structure. As it says on Jpred's result page (and help), in this case it might be worth looking at these homologues with experimentally determined structures for information on secondary structure. Most likely it will be more accurate ...


1

I might be wrong, but aren't numbers $n$ and $m$ are connected as $n=m+1$? Answer seems to be combinatorial: how many combinations of $n$ objects can be assembled under certain restrictions? Namely, how many isoforms certain gene can have. Restrictions include: how many exon-intron junctions on codon (or precisely between codons), how many exons are ...



Top 50 recent answers are included