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Questions tagged [proteins]

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

4 votes
1 answer
137 views

How to connect proteins via disulfide bonds computationally?

I want to connect proteins together to form a dimer. As seen in the picture, the monomers come close to each other along the edge of the higher-order structure (forget about the sulfate there). How ...
ste's user avatar
  • 662
5 votes
1 answer
235 views

Thermal stability of charged and uncharged alpha helices (the concept of alpha-helix capping)

I just learned that charged alpha helices are less thermally stable than uncharged ones. The only difference I see between them would be a larger dipole moment in the charged helix, but how would this ...
ste's user avatar
  • 662
5 votes
1 answer
585 views

Tandem mass spectrometry: a1 and immonium ions

In tandem mass spectrometry of proteins one will usually end up with a mix of $b$ and $y$ fragments but also $a$ fragments and immonium fragments. My problem is that wouldn't an $a_1$ ion be the exact ...
Matthieu Kratz's user avatar
6 votes
1 answer
233 views

Protein purification with Cobalt

Cobalt exhibits a more specific interaction with histidine tags, resulting in less nonspecific interaction than nickel. For this reason, cobalt is the preferred divalent cation for purifying His-...
Plutonium94's user avatar
2 votes
1 answer
301 views

Hydrolysing large molecules to reveal amino acids

Consider Oxytocin: I am asked to hydrolyze Oxytocin and reveal 5 amino acids which are the result of this hydrolysis. I must admit I have no idea where to begin. I know that generally amino acids ...
Paze's user avatar
  • 703
3 votes
1 answer
1k views

Denaturing of Proteins and Nucleic Acids - Effect of Temperature (Heating vs Cooling)

Heating a protein/nucleic acid will disrupt inter-molecular and intra-molecular forces in the tertiary structure. It will also interfere with the shape of the active site if the protein. Does this ...
confused's user avatar
  • 751
0 votes
1 answer
191 views

How does formylation of a nitrogen change the hydrophobicity of a target protein?

How does formylation, of the sort shown here: (from this Wikipedia page) affect the hydrophobicity of the target protein? Can we say anything general about adding a formyl group to a nitrogen?
GKT's user avatar
  • 1
6 votes
1 answer
990 views

Is there a chemical test for gluten?

I am looking for a chemical test for the presence of gluten: however, having looked online for such a thing, all the results seem to be about 'home testing kits' (presumably for people with a gluten ...
user5374's user avatar
3 votes
2 answers
121 views

Explaining a biochemical reaction (protein labelling, e.g. with fluorescent probes)

I am an immunology master student without prior knowledge of biochemistry. Could someone explain to me the following 6 reactions? What I want to understand is why exactly the reactions happen at this ...
reBourne's user avatar
4 votes
1 answer
15k views

Can acidic conditions break disulfide bonds

I am denaturing a protein using organic solvent and acid (49:49:2% water:methanol:acetic acid), but I want to maintain the disulfide bonds. My chemistry knowledge isn't good but disulfides are broken ...
Anake's user avatar
  • 143
25 votes
1 answer
2k views

How can I determine if there are π-π interactions between an amide and an aromatic ring in a protein?

In a crystal structure I've determined, a triazole ring on my ligand appears to be stacking with a tyrosine (top in picture): However, there is also an amide, courtesy a glutamine, near it (bottom). ...
Nick T's user avatar
  • 2,573

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