

BabcockHall
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Everything posted by BabcockHall
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A good place to start is to define what you mean by V0. Then you can see what information is needed.
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By G3P, what do you mean? What are your thoughts with respect to this question? For your other questions, I think you will have to look into the stoichiometry of how many electrons it takes per ATP synthesized.
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What are your thoughts? We don't just dump answers to homework problems here.
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Thermogenesis without shivering
BabcockHall replied to Nomegusta's topic in Biochemistry and Molecular Biology
The favorable movement of electrons from NADH to oxygen is coupled to the unfavorable translocation of protons across the mitochondrial membrane. The return of these protons through ATP synthase is coupled to the synthesis of ATP. Some substances, such as dinitrophenol, are poisonous because they act as uncouplers. Do you happen to know how they work? Thermogenin works in a similar manner, although one might argue that it is not an identical manner. The cytochrome proteins of the mitochondria are partially responsible for the brown color. -
Thermogenesis without shivering
BabcockHall replied to Nomegusta's topic in Biochemistry and Molecular Biology
Do you have any thoughts on how it might happen? Do you know how ATP is mainly synthesized in mitochondria? Maybe one place to start would be what causes the brown color. -
Of course it is unethical.
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I wonder whether the peak at 2.09 ppm might be acetone. Some people clean their NMR tubes with acetone, and so seeing a little residual peak from it is not impossible.
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My guess is that the 1.43 ppm peak is water in the deuterated chloroform (which is unlikely to be completely dry), but I don't see a residual HCCl3 peak near 7.26 ppm. Did you use CDCl3 as your NMR solvent? If you had some ICHD2 it would show up as a 1:2:3:2:1 pentet. A C-13 spectrum might not be a bad idea, especially if your present sample is at sufficient concentration.
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Connection between metabolism of fats and carbonhydrates?
BabcockHall replied to Nomegusta's topic in Homework Help
The question is huge. A proper answer could be found by reading specific portions of several chapters in a standard biochemistry textbook. -
I agree with CharonY. For many common antibacterial solutions, there are tables that provide concentration ranges at which the compound is typically used. These tables may be found in reference books such as Sambrook et al. However meropenem is unfamiliar to me, and I don't recall having seen it in any table with which I am familiar; therefore, some of these tables may not be what your need.
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Exotoxins are released from the cell, but endotoxins are not. Endotoxins are either on the cell surface or are intracellular.
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I could be wrong about this, but perhaps the chemical shift is concentration-dependent. As the concentration of water in the chloroform increases, there is more opportunity for hydrogen bonding. I don't have a citation handy, however.
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Good afternoon, We have a been working on a phosphatase, which gives indifferent over expression levels in E. coli using a T7-based system. We also have a triple mutant variant which also does not express well. Both proteins are trickier to purify than other proteins with which I have worked, because they seem prone to precipitation. We have not yet found conditions which reliably keep them in solution at concentrations above roughly 2 mg/mL. More recently we were given a plasmid with the phosphatase as a GST fusion, and it over expresses well. We are wondering what is likely to be the best way to obtain a gene for our triple mutant as a GST fusion. We see two basic alternatives: A. site-directed mutagenesis of the GST fusion we already have. B. recloning of the triple mutant that we now have in to a GST-based plasmid. We are in the process of obtaining the sequence of the triple mutant but do not have it at the moment. I don't have any prior experience cloning into systems using affinity tags (my cloning skills in general are quite limited and out of date). I have consulted Amersham's GST fusion handbook (specifically Chapter 2). However, it is not very specific about how to obtain a plasmid with the insert in the correct reading from. Does anyone have an opinion on which strategy is likely to be better? Does anyone have a good resource for information on cloning into GST fusion plasmids. Thank you for your time.
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It is difficult to be certain what your question is. Is the enzyme a phosphatase? Many phosphatases take para-nitrophenylphosphate as a substrate and produce para-nitrophenol as a product. Is the para-nitrophenylphosphate dissolved in 1 mM HCl. Or do you mean that the para-nitrophenol is dissolved in 1 mM HCl? What do you know about the acid-base chemistry of para-nitrophenol? What do you know about the UV/VIS spectrum of this compound?
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What makes you think that spider's web protein is water soluble? With what does ninhydrin react?
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There are many examples of how hormones (and also certain intracellular signals) regulate oppositely directed enzymes in a reciprocal manner. The most obvious examples are phosphofructokinase-1 and fructose 1,6-bisphosphatase and how fatty acid biosynthesis is regulated at its first committed step in eukarotic organisms. The paired enzymes of glycogen anabolism and catabolism are also well-studied.
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I am not sure what you mean by "example of fatty acids entering TCA from anabolic reaction." Fatty acids do not enter the TCA cycle from an anabolic reaction; they enter after beta-oxidation, which is catabolic. Do you think that the question wishes you to discuss the joint regulation of anabolic and catabolic pathways?
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If an aqueous reaction speeds up as the concentration of protons is increased, then it is subject to specific acid catalysis. If a reaction speeds up as the concentration of a buffering species is increased at constant pH, then general acid (or general base) catalysis may be occurring (but nucleophilic catalysis would need to be ruled out before one could conclude that it was IIUC). The key is that if one raises the concentration of a buffer then one does not change the pH (to a very good first approximation), yet the reaction speeds up. Therefore, the weak acid or weak base component of the buffer must be the catalytic species. William P. Jencks' Catalysis in Chemistry and Enzymology has a good discussion (all of Chapter 3), despite its being an older book. Many enzymes use a histidyl residue to perform general acid or general base catalysis; these include chymotrypsin and ribonuclease A. General acid and general base catalysis may be more important for enzymes than in organic synthesis, because much biochemistry takes place near neutral pH, where both protons and hydroxide ion are in very low concentration.
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If the nitrogen were protonated, it would not have a lone pair of electrons to coordinate to the iron ion.