Questions tagged [proteins]

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

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What does the word "dynamics" mean in the context of proteins or biomolecules in general?

What does it mean by “dynamics” when we say “dynamics of protein” or “dynamics of biomolecules”? For instance, McCammon's paper has the title "Protein Dynamics" [1]. What does the word “...
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What are the available cheap proteins that are much less soluble than BSA

Currently, as a beginner, I'm performing solubility analysis (with UV based spectrometry) for practices. The protein I'm using now is BSA. This is widely used and cheap option. I'm now looking for a ...
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Can we compare absorbance of two peptides when the read concentration from Qubit Protein Assay are different?

I have two peptide A and B. And I would like to know the solubility level of these peptide in certain solute. For that purpose I use Qubit Protein Assay. The Qubit readout I get is this: Note that ...
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How to calculate concentration of a protein based on known concentration and mw of other protein

I have a Peptide A (mw = 5074Da), the table below showed measured concentration by Qubit from 5uM up to 80uM solution. All under 20uL solution. Below is the standard plot for Peptide A (not sure if ...
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Why does a big protein move during gel electrophoresis but to a lesses extent through a size exclusion column?

A big protein going through gel electrophoresis will be forced through the gel, it will drift a small way and will show on the top of the gel, while in size exclusion, the big protein is not forced to ...
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Spectroscopic methods for quantifying peptides/proteins with or without Tryptophan or Tyrosine content

I have several peptides (20-50 amino acids long) which I want to quantify the solubility/concentration in a solvent at certain temperature and pH. These peptides may or may not contain Tryptophan or ...
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How does protein denaturation speed change with temperature? [closed]

So this is something that I had been wondering since middle school. We "roughly" know that protein denaturation occurs above a temperature of 72 degrees Celsius, and is the reason why it is ...
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2 answers
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Is the 3D spacing arrangement of atoms in chemical bond always unique?

I would like to ask if the 3D spacing arrangement of atoms in chemical bond configurations are always unique, please? For example, glycine consists of the set of atoms HHNCHHCOOH. Does there exist a ...
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Best description of forces/ mechanisms that stabilize the interaction between a hydrophobic protein binding pocket and a hydrophobic ligand

This is a more theoretical or definition question that is related to the terms "hydrophobic effect", "hydrophilic interaction", and "van der Waals' forces" (and others I ...
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How does ethanol separates salts from proteins [closed]

Grad student here messing around with famed TRIzol isolation protocol and looking to optimize the protein yield at the end. There are more direct ways to get protein from a sample but I like getting ...
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Troubleshooting an Autodock Vina Error on Chimera: "Could not find an atomic number for Hn Hn"

After having minimized a ligand (that I prepared on Marvinsketch), and after having prepared a target enzyme to dock said ligand onto (collected from RCSP PDB), I was met with an error by the reply ...
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Q-TOF vs Q-orbitrap MS data

I recently had the opportunity to analyze the same (intact protein) sample on an Agilent QTOF and a Thermo Q-Exactive, and noticed that in addition to having a moderately higher resolution the ...
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Loss of entropy and solvation energy in proteins

I am reading a chapter on protein stability. One section outlines the role of salt bridges or ion pairs in the stability of a protein. The excerpt goes as follows (italization added for emphasis): ...
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What are the initial experiments to hypothesize or decide the method of protein degradation?

For a protein of interest, How to determine it’s degrading method— protease or proteasome? Is it possible through bioinformatics? What are the initial experiments to hypothesize or decide the method ...
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What do sequence numbers in PDB files actually mean and why don't they match the sequence?

I am studying the 3D structure of the LDH from x-ray crystallographic imaging I was pointed to from Is there any stereospecific enzyme in PDB that catalyzes an anabolic reaction and has an entry ...
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Hypothetical Alternative for Nitrogen [closed]

Recently I was surfing the internet and I found thisWikipedia article. It states that The element silicon has been much discussed as a hypothetical alternative to carbon. Silicon is in the same group ...
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What is "tail" in case of secondary structure of protein? [closed]

What is a "tail" in the case of the secondary structure of a protein? How does it influence the "protein assignment" task?
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How do I obtain a 3D MOLFILE for the lactose synthase structure, especially the catalytic center?

So for example there is a paper by Ramakrishnan and Qasba which presents a model in a 3d stereo picture it has UDP-Gal, Glc, Mn++, a piece of the lactalbumin protein (?) and a piece of the lactose ...
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How can all amino acids point outwards from an alpha helix, if peptides are mostly trans?

My textbook in biochemistry ("Biochemistry" - Berg,Tymoczom Gatto, Stryer) tells me that: "Almost all peptide bonds in proteins are trans" (p. 40) At the same time, it states the ...
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Lysozyme crystals versus NaCl

If someone has some experience with lysozyme crystals I would be interested in knowing whether any of the images below seem likely to be lysozyme. Solutions were made with powdered lysozyme ($\pu{50 ...
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What do natural hybrids of peptides and nucleic acids look like?

Until recently I thought that there was a clean distinction between polypeptides and oligonucleotides, but apparently there are recent studies of therapeutic compounds that could be described as "...
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Mechanism of Action of Carbachol

Carbachol (carbamylcholine chloride) is known to be a cholinergic agent. Does it work as an indirect agonist by inhibiting acetylcholinesterase, as a direct agonist of acetylcholine receptors, or is ...
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What does it mean by spatial neighbor?

What does it mean by a spatial neighbor (SN) in the case of a protein residue or protein chain? Why is it different or special as opposed to other neighbors?
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3 votes
1 answer
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What is the maximum length of peptide which considered to be hard for synthesis by the current technology?

I am a molecular biologist and work with recombinant proteins. I am wondering what the cut point, in terms of length, is at which I should produce the peptide using heterologous expression rather than ...
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2 votes
1 answer
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How to identify 'water' mistakes in protein crystal structures: Are B-factors and occupancy good indicators?

When solving the structure of a protein from diffraction data (x-ray crystallography), it can sometimes be difficult know what should be modelled into small spheres of electron density that are not ...
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1 answer
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What does the following diagram represent?

Suppose, the following is a diagram of a protein's polypeptide chain: What does this diagram represent? What are the letters A, E, M, W, L, N, S, etc. represent? (I suppose these are amino acid ...
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Can Amphotericin B cross a lipid bilayer membrane in its zwitterionic form when it is loaded in the aqueous core of a liposome?

Can Amphotericin B cross a lipid bilayer membrane in its zwitterionic form when it is loaded in the aqueous core of a liposome? Or must it be uncharged in order to cross the lipid bilyer membrane of ...
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-1 votes
1 answer
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Protein drug conjugate exercise

I am supposed to draw the structure of a derivative of the following structure which could be used to make a protein drug conjugate. And then I should draw the reaction for the protein modification. ...
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4 votes
3 answers
315 views

What is the difference between structure assignment and structure prediction?

I am absolutely new to structural bioinformatics (only started last week). I am working on the secondary structure assignment/prediction (actually I am not sure) of proteins using machine learning. ...
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1 vote
2 answers
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To which extent is protein folding conserving subprotein structures?

I am actually a pure mathematician, who stumbled over this paper «Protein-Folding Analysis Using Features Obtained by Persistent Homology» by Ichinomiya et al. (Biophys. J. 118, 2020, 2926-2937; link),...
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7 votes
1 answer
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In solid-phase peptide synthesis, why are the formation of aspartimides a problem but not "glutamides"?

I'm studying solid-phase peptide synthesis (SPPS) at the moment, and a common problem is the formation of aspartimides, which disrupt the synthetic process. I understand how they form and why are they ...
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SARS-CoV - relative size of the spike protein

I am taking an online course in image analysis and have been asked to use the attached image to determine the size of the SARS-S protein of the SARS-CoV relative to the total of its proteins. However, ...
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Is there a computer program capable of showing protein conformational changes based on pH?

As it is known, changes in pH change the attractions between the groups in the side chains of the protein. Acidification can, for example, cause protonation of the $\ce{COO-}$ end to $\ce{COOH},$ ...
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7 votes
4 answers
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Ramachandran plot Phi(ϕ) Psi(ψ) dihedral angle Convention for Zero, Positive and Negative value- old and new

Update: possible duplicate: What is the precise definition of Ramachandran angles?. Question modified. G.N. Ramachandran et al, in their own work (PMC) (DOI), did not used phi(ϕ) and psi(ψ) as we use ...
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Carbon atoms types in amino-acids [closed]

I'm looking for a table or another kind of schema where I can find which type of carbon atoms (sp3, sp2 etc.) are present in each amino-acid. In my biochemistry books these informations are not ...
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1 vote
1 answer
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Do phosphoryl thiocholines, their uncharged analogs, and other organophosphates, interact differently with Acetylcholinesterase?

As asked in the title, would the various salts -such as hydrochloride or methyl iodide- of V-Agents interact any differently with acetylcholinesterase compared to the neutral compound? For instance, ...
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1 vote
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How carbon nanotube sensors works?

How carbon nanotube sensors works? Is the protein (or chemical compound used as part of the sensor) placed inside the tube or where is it placed? and how is the technology used to place the protein ...
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2 votes
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Differences in AChE inhibition kinetics between paraoxon and methyl paraoxon

According to literature, dimethyl paraoxon has a reaction rate constant for the aging (spontaneous dealkylation) of acetylcholinesterase of $\pu{0.186 h-1}$, a spontaneous reactivation rate constant ...
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3 votes
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Differences in AChE inhibition kinetics between VX and VR

According to the referenced paper, VR has an AChE inhibition reaction rate constant almost 4 times that of VX. Interestingly, its reaction rate constant for aging of the enzyme is less than that of VX,...
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4 votes
2 answers
471 views

Why does denaturation of albumen protein cause pH of solution to increase?

I'm interested in the denaturation of proteins by alcohols, specifically by ethanol. I have devised a simple experiment in which I inject solutions of ethanol (of variable concentrations) into ...
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How can DI water inhibit peroxidase activity?

I'm troubleshooting an IHC staining issue, and according to Thermo-Fischer's website, "Deionized water can sometimes contain peroxidase inhibitors that can significantly impair enzyme activity.&...
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2 votes
1 answer
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Determination of metal state from protein X-ray structure

Many proteins or enzymes contain metal ions within their active sites. These metals are often directly involved in the reaction catalysed bu the enzyme. In certain cases the function is well known and ...
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1 vote
1 answer
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Depicting a mechanism of peptide bond formation with protonated and deprotonated amino group

I've noticed that some textbooks and video lectures use an amino acid wherein the amino group has two hydrogens, and others use an amino acid with three hydrogens in the amino group (in the formation ...
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Why is Chlormephos highly toxic despite requiring metabolic activation?

According to the book "The Chemistry of Organophosphorus Pesticides", the insecticide Chlormephos (S-(chloromethyl) O,O-diethyl phosphorodithioate) has an oral LD50 in rats of 7 mg/kg. For ...
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7 votes
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Are all protein tetramers considered to be "dimers of dimers"?

Is every tetramer thought to be a dimer of dimers? Because even if every subunit is unique in structure, it could be a heterodimer of heterodimers? Or is the term "dimer of dimers" reserved ...
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Right conductivity of protein sample for Protein A purification of human IgG?

A sample from a cell culture has some IgG and this is to be purified using protein A chromatography. Based on the chromatography handbook from GE-Healthcare/Cytiva, the protein sample should have &...
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4 votes
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Why are isomers of parathion less active acetylcholinesterase inhibitors than paraoxon?

Parathion itself has been found to be a very weak inhibitor of acetylcholinesterase. It normally requires metabolic activation and the conversion into paraoxon in the body to actually start exhibiting ...
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What is the chemical reaction behind ginger milk curd?

Pouring hot milk into ginger juice solidifies the milk. All I know is that ginger juice contains Zingibain that could break down milk proteins into smaller polypeptides. I'm confused as though why is ...
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5 votes
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Why are S-thiocarbamates less toxic than carbamates?

According to Haley and Rhodes, neostigmine bromide (alternatively known as Prostigmine) has an LD50 in mice of around 0.165 mg/kg by IV injection. Pubchem claims that this is also the LD50 for ...
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2 votes
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Molecular dynamics simulation of a protein in acidic medium

I want to perform an MD simulation of a protein under acidic solvent conditions. A quick literature search seems to indicate that people are more interested in the protonation of protein side chains (...
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