All Questions
Tagged with proteins biochemistry
108
questions
4
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3
answers
206
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How is it known that proteins are polymers of amino acids?
I read the following here.
In 1902, Emil Fischer and Frank Hofmeister independently proposed that proteins are formed from many amino acids, whereby bonds are formed between the amino group of one ...
- 109
3
votes
0
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38
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Assessing stability of protein used for interaction experiments after changing buffer from tris to HEPES
I have a protein with a theoretical $\mathrm{pI}~9.0$ currently stored in $\pu{25 mM}$ tris and $\pu{250 mM}$ $\ce{NaCl}$ $(\mathrm{pH}~8)$ at $\pu{−80 °C}.$ I need to do experiments in HEPES at $\...
- 488
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40
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What is the industrial alternative to dialysis?
I want to separate a recombinant protein from imidazole. Both of them are in a solution of pH 8. I was thinking of using ion exchange chromatography with cationite: the imidazole being positively ...
- 109
2
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0
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Reason for differences in AChE aging/reactivation kinetics between neutral and charged organophosphorus inhibitors
According to the referenced papers, acetylcholinesterase that has been inhibited by an organophosphate possessing thiocholine as its leaving group is more susceptible to reactivation by oxime ...
- 1,264
2
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1
answer
88
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What can I do if a peptide won't go in solution in a biological assay?
I have working on the realisation of on assay, that is intended to examine the activity of a protein. The assay works in a way, in which the product of the target enzyme is transfered by a support ...
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3
votes
1
answer
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Effect of presence of competitive inhibitor on observed reaction constant
Suppose there is a solution of enzyme, its substrate, a competitive inhibitor, and a suicide inhibitor. The reaction rate constant for the reaction of the suicide inhibitor with the enzyme is known. ...
- 1,264
3
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1
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174
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Effect of competitive inhibitor on substrate inhibition
In an enzyme that undergoes substrate inhibition, how would the presence of a competitive inhibitor affect said substrate inhibition? Would the substrate concentration at which substrate inhibition ...
- 1,264
2
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0
answers
39
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How are enzyme inhibition constants assayed for "multi-inhibitors"?
Suppose there is a suicide inhibitor of an enzyme that reacts with the enzyme to form an inactive enzyme and another product. This "Another product", however, is capable of acting as a ...
- 1,264
2
votes
2
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145
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Does the word "restraint" have any special meaning in the case of protein or biochemistry?
The following screenshot is taken from the book The Encyclopedia of Physical Science & Technology, volume: Biochemistry, Edition: 3rd, Page-197.
The text says:
FIGURE 3 Schematic representation ...
user124269
1
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0
answers
31
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Why is AChE inhibited by triflates not susceptible to reactivation?
According to a report, certain esters of trifluoromethanesulfonic acid are capable of acting as irreversible inhibitors of acetylcholinesterase. Also, 3-PAM, while capable of reactivating AChE ...
- 1,264
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71
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Do whey proteins precipitate with heat?
I am currently studying about the biochemistry of yoghurt and when reading about the effect of heat in milk proteins specifically whey, my book says that heat can denature whey proteins.
So after the ...
8
votes
1
answer
311
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Why is collagen fibre autofluorescent?
Why is collagen fibre autofluorescent? Proteins with increased amount of trp, tyr, phe tend to fluoresce but I don't think collagen fibre has increased percentage of any of them. Some say collagen ...
- 197
1
vote
3
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407
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Why do hydrogen bonds between atoms of the polypeptide backbone, form both helix and pleated structures, instead of only one structural type?
Proteins have segments of their polypeptide chain/chains that can be repeatedly coiled or folded into helix and pleated structures, respectively. This is due to hydrogen bonds between partially ...
- 67
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2
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567
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Why are proteins made up of alpha amino acids and not beta amino acids?
Why are proteins made up of alpha amino acids and not beta amino acids? Or gamma amino acids? My idea on this would be that a world with beta or gamma amino acids would be too complicated? Is that ...
5
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70
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Do disulfide bonds determine the 3-dimensional structure of a protein or do they just stabilise the 3D structure?
I noticed that most disulfide bonds occur when two cysteine side chains exist in close proximity to each other. Do those cysteine side chains "look out" for each other during folding, that ...
- 107