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Are multi-chain proteins synthesized as one biological unit? Sometimes yes but mostly not. Some proteins are synthesized as one long polypeptide pre-protein which is cleaved by some proteases to yield multiple chains. After cleavage the intramolecular interactions become inter-molecular or inter-chain interactions. Insulin is a good example of this ...


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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 ...


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What you need to do is compare the relative amounts of the protein in the insoluble (pellet) fraction to the soluble (supernatant) one. This way you can determine how soluble the RMAS has become through the effect of the indicated compound. DTT breaks disulfide bonds, but does nothing else to solublize the protein, so it's all in the pellet, with none ...


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Some experimental and modelling observations suggests, folding energy for right handed in more favorable. You can find more detailed answer to this question here.


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As far as I know, microscopy (be it with dyes like fluor or with genome-encoded calcium indicators) is really your only good bet, especially for getting quantitative sensitivity, which I think is what you're looking for. Changes in cytosolic calcium are incredibly dynamic both in time and space, which is something to consider when asking how calcium affects ...


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This question is waaaay too broad, but I'll give some short and simplified answers to the hypothetical you asked at the end. First, let's reformulate your example a little bit: How does the ribosome move along a strand of RNA? How would it do it? By hydrolyzing GTP and somehow coupling the free energy associated with that reaction to forward motion. ...


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This isn't a question with a really well accepted answer yet, and comes up quite a lot in e.g. studies of population variation in transcription factor motifs. Usually, we approximate the sequence preferences of a DNA-binding protein with a position weight matrix. A weight matrix will given you a score for two sequences, so the simplest means of quantifying ...


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First: You are right with your reasoning that Protein X (X) and Dcr-2 interact directly. Lets go through the blots: In the input you check for the proteins loaded into the setting and stain unspecifically with Coomassie. This part of the blot shows you no unspecific input, and both proteins of interest present. This also shows that Dcr-2 is much bigger than ...


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As it seems with about everything in protein science, the answer is it depends on the protein. Many proteins will lose activity if they are truncated; however, I've worked with GPCR's that were truncated down to the extracellular portion only and they showed consistent kinetic results. Antibodies have been cut into pretty tiny chunks (scFv's) to create ...


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As @canadianer mentions in his comment, Protein G is more than likely named after the human group G strain of Streptococci, G148. Protein G, a bacterial cell wall protein with affinity for immunoglobulin G (IgG), has been isolated from a human group G streptococcal strain (G148). Purification and some properties of streptococcal protein G, a novel ...


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You are seeking a database of transcription factor binding specificities. Some model organism databases (which are manually curated), such as Wormbase contain some of this annotation. I suggest you search PubMed for papers by Tim Hughes at the University of Toronto. He has published extensively on this topic over the past 5 years. Papers he cites, and ...



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