Biopolymers consisting of amino acids that fold into 3D shapes and perform a large number of functions in living organisms.

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Amino acid compatibility

The (human) genetic code encodes 20 amino acids. They form a protein using peptide bonds. Each amino acid has a carboxyl group (COOH) and an amino group (NH2) that can potentially form a peptide bond. ...
6
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2answers
549 views

Solvent Accessibility, the 20% cut-off method

I'm reading the papers linked below and all three of them mention a 20% cut-off for buried/exposed residues, by calculating a relative solvent accessibility (RSA) value. I understand how the RSA is ...
4
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2answers
116 views

Proteins that give color (without fluorescence)

Is there proteins that have strong color, that could be seen without the need of UV and with naked eyes (with white light) - in mammalian cells? Searching for reporter, something like GFP, but that ...
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1answer
39 views

Using Jpred to predict secondary structure

I'm trying to use Jpred to predict secondary structure for a protein sequence. When I run J-pred, I get a bunch of hits from PDB. I've also noticed these 'hits' are the same name as the templates i ...
0
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1answer
32 views

One Gene and many proteins [closed]

Imagine a gene with $n$ exons and $m$ introns. How many proteins are possible from that gene? Would all the proteins be isoforms?
1
vote
1answer
47 views

Which protein complex is composed of the greatest number of different kinds of proteins, and how many types are involved?

Why are some protein complexes composed of many different types of proteins? How many different types are they composed of? In particular, which protein complex has the greater number of different ...
3
votes
1answer
67 views

Why do some proteins “use” a beta barrel structure instead of alpha helices in transmembrane space?

Most proteins are fixed in the membrane by alpha helices. But some use beta barrels. Wikipedia describes beta barrels as used for porins, preprotein translocases, and lipocalins. To me, a coiled coil ...
4
votes
1answer
29 views

Are all protein composed of all the amino acid (in animal) or are there less diverse protein?

I have a question about amino acid composition of proteins: Are there proteins in animals that are made up only from a small subset of amino acids? So instead of all 20 amino acids let's say only 6-14 ...
5
votes
2answers
1k views

What has caused life to choose this unfathomably tiny subset of all possible proteins?

I wonder why life uses the particular proteins that it does, about 10^6 different proteins, I think? Evolution cannot explain it because the number of possible proteins is far far too large to ever ...
14
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4answers
977 views

How many human proteins have a solved 3D structure?

I was wondering how many human proteins have a solved 3D structure. Is there a database with only human proteins? I looked at pdb but couldn't find a filter.
6
votes
2answers
514 views

What is the purpose of using two layers of gel in SDS- PAGE?

I just made a SDS-PAGE with a top layer of stacking gel and a bottom layer of separating gel with different pH values of 0.5M Tris-HCl. The stacking was 6.8 and the separating gel was 8.8. What about ...
0
votes
1answer
49 views

What is a complex?

In my text book it says that "Troponin" is a complex of Troponin C, I and T. In this sense, what is the relation between Troponin complex and C, I, T?
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0answers
45 views

Best software for protein in electric field modeling?

I'm trying to find a free, or cheap, software program to model the movement of a heterotrimeric protein in an alternating electric field. The dipole and crystal structure of the trimer are known. ...
0
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0answers
13 views

About post translational modifications

A secreted monomeric protein of 132 amino acids, lets say protein XY, has two N-linked glycosylated Asparagine residues, at position 10 and 67, and act as a ligand for a XY-Receptor (XYR). I want to ...
3
votes
0answers
19 views

Is there a cellular mechanism that detects Ribosomal damage?

What kinds of options, if any, do cells (Eukary and Prokary) have for detecting, and repairing damage in Ribosomes (of all types)? I am curious as to what happens when a cell sustains damage of some ...
4
votes
1answer
52 views

How can human infants express chymosin with only a pseudogene at their disposal?

I read on the Wikipedia article about Chymosin http://en.m.wikipedia.org/wiki/Chymosin It stated that chymosin is produced by gastric chief cell in human infants. But it also stated that human only ...
1
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0answers
23 views

Question about cytoskeleton coordination

I am trying to study for a biology and I am having some confusion over the following topic. Can anyone help explain/ shed some light on the concepts of Rho family GTPases. Is it true that we have Rho ...
1
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0answers
36 views

Compare Proteins - Structural / Sequence parameters

I have been working on algorithms that extract co evolutionary signatures from protein sequence. As a result of my work I got some evolutionary information which possibly explains cotranslational ...
7
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3answers
12k views

Why are 3 nucleotides used as codons for amino-acid mapping in DNA?

DNA is made of 4 unique nucleotides. When coding for a protein, a sequence of 3 nucleotides is used to code for each amino acid. Why are codons 3 nucleotides in length? A related question can be ...
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30 views
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0answers
22 views

Where does the oxygen and water produced from the decomposition of hydrogen peroxide by catalase enzyme go?

How are they disposed of by the body, or are they disposed of at all? Since our body needs water and oxygen anyway, I'm speculating that these "waste product" will be reused/recycled by the body in ...
5
votes
1answer
193 views

Where do amino acids get attached to tRNA and where is it synthesized?

Some very basic parts of transcription/translation seem to be left out in various literature. I can't find the answer to this anywhere: How exactly is tRNA synthesized? I realize that mRNA is ...
4
votes
2answers
194 views

Why proteins are not visible on my membrane after ponceau staining?

I have a problem in western blot that I can't resolve by myself. When I am use to add 100 microgram of proteins for each sample but after running and transfer its impossible to me to see bands of ...
2
votes
1answer
57 views

Is it possible that a set of functionally related proteins in a pathway fulfill different functions? [closed]

Could it be that a given pathway of enzymes (or proteins in general) may fulfill different purposes in a cell by for shifting partners? Say protein A activates B, B activates C and C has a specific ...
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0answers
40 views

How do BCAA's promote faster muscle recovery?

I am aware that ingesting Branched chain amino acids (BCAA's) prior, during, and after workouts has an effect on muscle recovery due to their difficulty of metabolism. However, how much more ...
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0answers
23 views

Incremental denaturation of protein mixtures

When a protein solution is heated above the denaturation temperature, it seems that denaturation does not happen at the time the temperature is reached, but it takes some time. I assumed that ...
5
votes
2answers
118 views

What percentage of a cell's volume is occupied by protein?

I was looking at one of David Goodsell's illustrations of a cell: And it seems to suggest a very crowded picture of the intracellular environment. Just how crowded are cytoplasms? What percentage ...
0
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0answers
71 views

Medical Uses of toxic venom

One interesting thing I recently learned is that venom has medical uses that can actually save lives! But from what I see so far this either applies to venoms from creatures that are not fatal to ...
2
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0answers
60 views

Are there sterilisation methods that do not denature proteins as heat does?

Context: Most countries require milk to be sterilised through radiation or heat to remove possible harmful bacteria. Both of these processes denature the proteins in the milk (ref). Are there methods ...
3
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0answers
112 views

Can't resolve protein with native PAGE

This is a native gel. Let's call the left 2 lanes protein A and the right 2 lanes protein B. B is the same as A except it has a FLAG tag. They are both homotetramers of about 65 kDa. After ...
2
votes
1answer
54 views

Edman method to identify peptides with Phenylisothiocyanate (PTH)

We all know that in this method the PTH reacts with the first amino acid (aa) from the N-terminal to the peptide and separates from it giving PTH-aa so that we can know the amino acids sequence in the ...
6
votes
3answers
224 views

Proteins folding

Some of us are involved in the folding@home project, spending time, money and resources. I would like to know an answer to two main questions: how do we know we fold it right? I mean these models ...
3
votes
1answer
76 views

Proteins in Milk, Oat , Eggs and Soy

I have read that there are proteins in oat which are similar to those in soy, milk and eggs. I know nothing about biochemistry, and I'm struggling to decipher the info i find.. the closest Ive got to ...
3
votes
1answer
132 views

What happens to the precursor protein's signal sequence after it is cleaved?

Where does this signal sequence "go" after it has been cleaved by signal peptidase and what is its next function?
3
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0answers
26 views

Is it possible to isolate and analyse intermediates of protein folding?

I would like to know if there is an assay which could allow us to analyse a protein before it has assumed its 3D functional form. While studying structural biology, I only came to know the forces that ...
2
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1answer
49 views

Protein PTM site prediction

Is there any in silico analysis method to predict post-translational modification sites on a given protein?
3
votes
1answer
42 views

Divalent cation binding to calmodulin

I have carried out a native PAGE with 4 reaction mixtures. To each I had added an equal volume of EDTA (1 µl/1mM) to sequester any divalent ions and an equal volume of calmodulin (5 µl/0.5 mg/ml). I ...
1
vote
3answers
93 views

What is the relationship between protein-protein interaction networks and metabolic networks? [closed]

I am trying to find out how these networks can be linked together. I know that Protein-protein interaction networks and metabolic networks both fall under the Intra-cellular type of biological ...
2
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0answers
56 views

How do I identify the protein with the highest Disulfide bond density? i.e protein with highest ratio of Disulphide bonds per Peptide bond? [closed]

I want to list all proteins in the protein database and list them by the ratio of number of disulphide bonds per peptide bond. I am not particular about the reliability of identification of ...
1
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0answers
46 views

Nutritious protein substance for vitamin enhanced crop?

I am not a bio or science major, but we have a subject, like an elective on biotechnology and we were tasked to think of a product that hasn't been invented yet. My groupmates and I thought of a ...
3
votes
1answer
46 views

IPTG and lac operator with e coli for foreign gene question

We did an experiment were we have e coli with a plasmid with a gene from another bacteria in it, and we put in IPTG in for induction. Will after looking up more about IPTG online I see it's related to ...
6
votes
1answer
48 views

Has the protein composition (with identification) in honey and other honeybee byproducts been studied?

I am interested in studying honey and other honeybee byproducts. I have not been able to find sequence or structure records for any of the contents of honey. In particular, I want to study the ...
2
votes
1answer
167 views

Proteins: Post translational modification

I am a physicist and trying to understand some protein chemistry for a small project. Basically, amino acids combine to form proteins and after forming the primary structure, some chemical ...
2
votes
0answers
50 views

Which method would more accurately help to identify the unknown concentration of a protein sample between the A280 and the Bradford methods?

I quantified my protein using the standard Bradford method and the A280 methods and obtained values that were far off from the theoretical value of the protein of interest, and therefore was wondering ...
3
votes
1answer
320 views

Do these things contain amylase? [closed]

I have 10 samples of some food or other things and I need to know, if it contains amylase. I already ran an experiment with storch and iodine, but I have to make it right and my experiment must not be ...
1
vote
2answers
46 views

How do I find a protein from this DNA sequence?

I have a DNA sequence from a sequencer. How can I determine what protein is it? I tried some translator but it didn't help. What protein is this and how can I determine it? The sequence: ...
8
votes
2answers
60 views

All UniprotIDs of a cancer pathway

I need to download all uniprotIDs of a cancer pathway, say the AKT Signaling. It may be super easy, but I don't know which resource to look at since it is a new field. How/where do I find these?
2
votes
1answer
156 views

Thermodynamics of Forming Peptide Bonds

Which of the following shows the correct changes in thermodynamic properties for a chemical reaction in which amino acids are linked to form a protein? A) +ΔH, +ΔS, +ΔG B) +ΔH, -ΔS, -ΔG C) ...
5
votes
2answers
178 views

What does units/mg mean for Streptavidin

I got streptavidin for surface reaction. The label says "biotin binding: 16 units/mg". What does units/mg mean? Does it mean "1 mg biotin can bind to 16 units ...
3
votes
1answer
76 views

How long does it take to form a peptide bond?

What is the time taken to form a peptide bond in vivo or in vitro? It isn't mentioned in my course on protein structures. I was just curious to find out if any time scale is known? Given that ...