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Questions tagged [proteins]

For questions about proteins. Proteins are biopolymers consisting primarily of polycondensated amino acids.

4 votes
3 answers
206 views

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 ...
powerful_bob's user avatar
0 votes
0 answers
40 views

Strange Binding Curve DNA:Protein Interaction

So I did some DNA:Protein Interaction studies using Fluorescence Polarisation Assays. I have fluorescently labelled DNA and add my Protein of interest. Down below you see an exemplary plot of the ...
TheChemist's user avatar
3 votes
0 answers
38 views

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 $\...
TheChemist's user avatar
0 votes
0 answers
40 views

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 ...
MathEnthusiast's user avatar
2 votes
0 answers
25 views

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 ...
user73910's user avatar
  • 1,264
0 votes
1 answer
111 views

Testing whether an unknown powder is wheat gluten (at home)?

Last week, I ordered wheat gluten to make seitan. I received some powder and attempted a recipe, which mixes 100g of water with 100g of gluten to form a sticky dough. However in my case, I only got a ...
Alduno's user avatar
  • 109
2 votes
1 answer
128 views

Calculate IC50 from fluorescence kinetic

I have an assay in which a fluorescence signal is generated when the enzyme reaction progresses. The fluorescence signal increases until a maximum is reached. Than it keeps constant. The first 1 h ...
raptorlane's user avatar
2 votes
1 answer
88 views

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 ...
raptorlane's user avatar
0 votes
0 answers
17 views

When optimizing AMBER molecular dynamics parameters for protein-ligand interactions, how do I balance accuracy and efficiency?

Are there established practices for fine-tuning AMBER MD parameters in scenarios like mine, involving specific factors like mutant proteins or non-standard ligands? Has anyone successfully tackled ...
Don Aborah's user avatar
-2 votes
1 answer
135 views

Non-toxic alternative to borax for use in slime chemistry?

I understand that sodium tetraborate decahydrate ($\ce{Na2B4O7•10H2O}$) and water is the primary binder for PVA glue based slimes. We have learned borax is not good for the ground water, or marine ...
Shannon Strong's user avatar
3 votes
1 answer
105 views

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. ...
user73910's user avatar
  • 1,264
3 votes
1 answer
174 views

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 ...
user73910's user avatar
  • 1,264
2 votes
0 answers
39 views

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 ...
user73910's user avatar
  • 1,264
6 votes
1 answer
153 views

Why Does Milk Seal Sidewalk Chalk?

I work at a public library and we recently had a sidewalk chalk hour for families. Someone gave us a tip that if we brush milk with a paintbrush over the finished chalk drawings, it helps seal them ...
Rachel's user avatar
  • 61
10 votes
1 answer
726 views

Why does this lysozyme powder not look crystalline?

I am very new to protein crystallography and visualization. I have been asked to take photos through an optical microscope of the lysozyme powder directly as-is from the supplier. I suspended some of ...
Mack's user avatar
  • 111
2 votes
1 answer
92 views

By what mechanism does amylase catalyze hydrolysis?

I've recently been learning bits and pieces of starch metabolism, and am wondering if anyone could explain exactly what is going on when alpha or beta amylase "cleaves" the 1-4 glycosidic ...
Matthew Finger's user avatar
2 votes
2 answers
145 views

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 ...
user avatar
2 votes
0 answers
71 views

Is there any special meaning to the angle between two peptide planes?

Take a look at the following image: Is there any special meaning to the angle between two peptide planes (marked with red arrow heads)? If so, why isn't a specific name (like phi, psi, etc.) given?
user avatar
1 vote
0 answers
31 views

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 ...
user73910's user avatar
  • 1,264
0 votes
1 answer
95 views

Is it possible to replace 3-mercaptopropionic acid with 2-mercaptoethanol to solubilize avian eggshell membrane to soluble eggshell membrane protein?

Is it possible to replace 3-mercaptopropionic acid with 2-mercaptoethanol to solubilize avian eggshell membrane (ESM) to soluble eggshell membrane protein (SEP)? Most literature suggested the use of ...
Aina Razali's user avatar
2 votes
0 answers
103 views

Protein/polypeptide nomenclature, residue number superscripted or not?

When referring to a specific residue number of a given amino acid, should the residue number be superscripted or simply affixed? For example, When referring to a Tryptophan residue at the 147th ...
sat0ri's user avatar
  • 161
0 votes
0 answers
71 views

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 ...
CaptainAmerica Whyso's user avatar
1 vote
0 answers
92 views

How come in biuret test the copper sulfate doesn't react with the sodium hydroxide?

As I understand the color change in the biuret test is due to the formation of a complex between the peptide (with more than 2 peptide bonds) and the $\ce{Cu^2+}$ ion, from $\ce{CuSO4}$. But before ...
CaptainAmerica Whyso's user avatar
8 votes
1 answer
311 views

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 ...
Yushi Li's user avatar
  • 197
1 vote
3 answers
407 views

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 ...
Growing6884's user avatar
0 votes
2 answers
567 views

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 ...
saturn20005252's user avatar
-3 votes
1 answer
49 views

what is the meaning by 'species' of glycine? [closed]

The question ask for the species of the (i) glycine hydrochloride (ii) glycine titrated with NaOH. When they mentioned 'species', what did they mean by it?
Nku's user avatar
  • 1
1 vote
0 answers
41 views

How to calculate absolute charge of a protein [closed]

My understanding is that hydrogen bonds formed by proteins require the NH2 / COOH to be neutral. Hence to find out when the hydrogen bonds are the strongest will depend on the absolute charge of the ...
TheRavenSpectre's user avatar
6 votes
2 answers
244 views

How is geometry optimization of small molecules different from the protein folding problem?

My layman's understanding is that finding the ground state geometry of small molecules is "hard". I don't have a good sense of how hard though. I suppose there are applications where methods ...
theQman's user avatar
  • 169
3 votes
1 answer
103 views

Contaminants in Ion Exchange Chromatography significance?

I am a high school senior and decided to do a project on the essential amino acid composition of varying vegan protein mixtures. I have run into a problem concerning protein purification. One of the ...
I do not want to put my name's user avatar

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