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- proteins - Why are prions in animal diets not destroyed by the . . .
Proteases are enzymes in your digestive system that help break down food, acting like molecular-sized scissors that cut up proteins Proteases have clefts, or subpockets, into which proteins fit, where the substrate (protein) gets cut Infectious or pathogenic prions are resistant to proteases, because of their three-dimensional shape, which hides away parts of the prion that would normally
- molecular biology - Does sample buffer require EDTA for protein . . .
Both steps ensure that proteases are either inhibited or completely denaturated, which will both protect the sample The only reason I can think of for using EDTA is that it can help to destabilize your target protein, when a co-factor which is important for the structure is complexed by EDTA and thus keep it in solution after the denaturation
- Difference between Peptone, Peptide and Proteose
In my school textbook, it is given that Pepsin converts proteins to peptones, proteose and peptides What is the difference between the three products? On googling the terms, the definition was s
- Why is pepsin able to operate at low pH? - Biology Stack Exchange
The reaction mechanism of pepsin, an aspartic protease, involves two aspartate residues, each of which has a low pKa, explaining why pepsin works optimally at low pH The catalytic mechanisms of other proteases (serine proteases and cysteine proteases) do not involve ionization changes in aspartic acid, which is why they operate at higher pHs
- Why do cell membranes have a lipid bilayer instead of a monolayer?
Many cells have a cell membrane composed of two layers of lipids Why is it that they have two layers and not just one? What purpose do this arrangement serve?
- Proteases in the blood - Biology Stack Exchange
Does having proteases in the blood mean the blood proteins are constantly broken down? How do the blood proteins get anything done then? And what good do binding proteins do in protecting hormones during vascular transit when the binding proteins are also susceptible to blood proteases?
- Does pepsin enzyme digest other enzymes like other pepsin molecules
Pepsin does cleave itself (Ingram, 1951) - this is termed autolysis Pepsin (and other proteases) act on proteins with the right amino acid sequences Pepsin prefers to cleave at phenylalanine, tryptophan or tyrosine residues (Lehninger, A Principles of Biochemistry) * Pepsin can also cleave inactive 'zymogen' enzymes to activate them One of these zymogens is pepsinogen (an inactive form of
- How exactly is casein digested? - Biology Stack Exchange
I mean it seems first step is rennin or pepsin digestion in stomach - then what happens with remaining peptides? I am interested in the whole process from casein to amino acids Is there brush bor
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