Answer:
Explanation:
1. charge in trypsin
: two other molecules in elastase
2. Chymotrypsin cleaves peptide bonds after bulky or aromatic side chains, such as those of the amino acids phenylalanine or tyrosine. The specificity pocket, or substrate-binding site, is deep and has hydrophobic side chains.
Trypsin cleaves peptide bonds following basic amino acid side chains. Lysine and arginine both have basic amino acid side chains that are positively charged at pH 7. Trypsin's substrate-binding site contains a negatively charged amino acid residue.
Elastase cleaves peptide bonds after amino acids with small side chains, such as glycine, alanine, or valine. The specificity pocket for elastase has bulky side chains that block larger amino acid side chains, but can accomodate smaller side chains, such as the -H, -CH3, and -CH(CH3)2 side chains of glycine, alanine, and valine, respectively.
3. Their binding pockets
- trypsin = long & (-) D on bottom
- chymotrypsin = deep & wide
- elastase = aliphatic a.a. = shallow
Each new dna double helix consists of one old dna strand and one new dna strand, daughter dna
Answer:
- They are made of denser objects, which can condense at relatively high temperatures;
- They are made of heavier elements, which have a stronger gravitational attraction to the Sun;
