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1

Let's do your second one first, you want to find the rate of binding: Yes you are right you need to calculate for km I think I found the paper that ties temp into the reaction rate: statistical approach called response surface methodology (RSM) is used for the prediction of the kinetic constants of glucose oxidase (GOx) as a function of reaction ...


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This sounds straightforward when thinking about it but finding hard evidence is not really easy. As this is too long for a comment, I have to put it in as an answer. Just a few thoughts: All enzymatic reactions are of course temperature dependent and usually have a temperature optimum at the specific living temperatures. For yeast this is around 27°C, for ...


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I agree with what MattDMo has said, but just to emphasise - a 'solution' or 'NMR' structure is not a crystal structure. ('Complex structure' probably means structure of a complex. e.g between a protein and a ligand.) To be a crystal structure the structure should be determined using X-ray crystallography. From the Protein Data Bank home page choose Advanced ...


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Depending on who you talk to (typically laymen and scientists who are not structural biochemists), the term "crystal structure" is frequently taken to mean "some determination of molecular structure, whether by actual crystallography or some other means". For example, a graduate student is talking to her adviser, an immunologist, about the ...


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In general, leupeptin (a cysteine, threonin and serine protease) and aprotinin (sometimes called Trasylol; trypsin inhibitor) are included in most mammalian cell lysate buffers. Whether you need them is really up to your protein of interest: if you know how it gets degraded in vitro, then you should be fine with inhibition of just those proteases. If instead ...


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The Ramachandran plot describes secondary structure. If you see a lot of beta sheets in your plot you will have a more compact molecule than one which is wholly alpha helix. Gly can be almost anywhere in any quadrant. Look for residues with secondary structure to determine tertiary structure.


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When φ = ψ = 180° the peptide is in the fully extended conformation i.e. it is the 'longest' it can be. If it isn't possible to deduce a length order based on this information then I guess you will have to do some geometry to calculate the sums of the distances between the α C atoms using the known values for all of the bond angles - ...



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