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
Answer:
- complex info; detailed instructions
genetic codes contain complex information; detailed instructions
Explanation:
The genetic code is a set of rules by which information encoded in the genetic material (DNA or RNA sequences) is translated into proteins (amino acid sequences) by living cells.
-The genetic code consists of 64 triplets of nucleotides. these triplets are called codons. With three exceptions, each codon and codes for one of the 20 amino acids used in the synthesis of proteins. that produces some redundancy in the code: MuscleTech amino acids being encoded by more than one codon.
The answer is B because each parent gives half of the genetic information
Explanation:
Option first is the correct one
