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I found article in Nature: A helper phage to improve single-chain antibody presentation in phage display Experimental protocol Standard cloning procedures, determination of colony-forming units and plaque-forming units, and immunoblot after PAGE were carried out according to Sambrook et al. Construction of the packaging cell line. ...


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in silico modelling of anything in biology is an active field of research. It's very useful for making predictions and developing hypotheses, but any findings need to be confirmed experimentally. From the Folding@Home website: Folding@home has been a success. In 2000-2001, we folded several small and fast folding proteins with experimental validation ...


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Fur, wool, and hair are all made of keratins. To the best of my knowledge wool and fur are separated arbitrarily, based on the properties of the fibres. This arbitrary division allows rabbits to have fur but selective breeding has produced angora rabbits, which have wool. The opposite should be possible, with time you could breed a sheep that has fur. ...


5

Surprisingly, the answer is yes. In 2012 Tanizawa et al published a paper titled Microorganism mediated synthesis of reduced graphene oxide films. The gist of it is that most of the steps (including the structuring of the graphene sheet) were carried out with chemical synthesis, but a final reduction step from graphene oxide to graphene was carried out using ...


3

I think I can help explain all but your 3rd question. A transgenic mouse will typically have the genetic construct in all cells. Unless you get a chimeric animal, which is screened for during the making of the mouse. VIP::Cre means that the promoter of VIP was used in front of the region of DNA that encodes for Cre recombinase. Note, the animal still has ...


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How far could we go towards engineering a space-durable human species? I think this question is likely to get closed as off-topic. It is extremely hypothetical and would be a better fit on WorldBuilding.SE. But here is my messy attempt to answer this question. Assumptions So, I guess in your question, you assume that we know everything about how our ...


3

Protein folding is a complex thing. There are huge computer algorithms and huge mainframes which are trying to predict the final 3D structure of a protein. Knowing the tertiary and the quaternary structure of a protein, allows us to understand why diseases happen. In many cases a mutation of the gene provokes an aberrant protein folding. When the protein ...


2

I will try answer your question directly. How do we know if we fold it right? A. If you're interested in only the end product pf folding -- the 3D structure, then this is the subset of the folding problem called the structure prediction (from sequence alone). a. We can verify the structure experimentally by determining the 3D structures by NMR or ...


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Yes, and no :-) In the meantime many protein structures can be predicted quite accurately - even those for which no reference fold had been known before. In this case the important buzz word is "big data": co-mutations (of charged amino acids) that can be found when sequencing many independent genomes. (... which indirectly bypasses the emphasis on ...


1

There are lots of things that you can eat that you could grow as a lawn. That probably are growing in your lawn now. My yard is about half violets and they are edible. Purslane is a delicious succulent lawn weed. Grab some, rinse it off and eat it. It is crunchy! I am telling you from experience you can eat a lot of it and you will not get sick. ...


1

You can try an evolutionary algorithm. If you can quickly evaluate the binding affinity you can initialize a set of copies of your protein but with random mutations. You can assign them a fitness score based on the affinity of the binding. The ones with highest affinity you replicate again with some probability of mutating each amino acid and you continue ...


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An article, Protein Misfolding and Degenerative Diseases, covers this question, and although it focuses on a single type of disease, this is of great importance. To summarize, there is the potential for misfolding in proteins because of the small differences in energy between different alternative folded states, and because during synthesis some proteins ...


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A certain fold of a peptide string can be validated or ruled out if other experimental data is available. Some other techniques to infer protein structure are X-ray crystallography (requires pure protein that will crystallize) and single particle analysis.


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One at a time, you could potentially label all of them. If you're asking how many proteins you could label at once, your biggest limitation is probably your microscope. In order to distinguish between different types of proteins you need different color fluorescent labels (dyes, fluorescent proteins, etc). Even the fanciest fluorescent microscopes tend to ...


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The fastest will change as time passes and better technologies are developed. I think the fastest method existing at the moment is Shotgun Mutagenesis (provided by Integral Molecular Inc). This does not employ any new method of doing that. They just provide a set of plasmids, that has all the possible mutations. The set itself is generated by automated ...


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