The skeletal muscles have striations to do their sacromere anatomy
sacromere which are formed by actin and myosin stacking
sarcomere is the functional unit of muscles and shows striated appearance due to thick and thin filaments
hope it helps
Answer:
<em> e) Ala</em>
Explanation:
Alpha helix is a secondary structure of proteins, it is made of 3.6 aminoacids residues per turn, this structure is possible thanks to local hydrogen bonding between C=O and N-h groups. The result is a cylindrical structure with a hydrogen-bonded backbone and the outside studded with side chains.
Glycin has an -H in its side chain, this makes it a too flexible molecule, therefore it's unusual to find them in alpha-helical structures because their presence could cause the helix to deform. Large R-groups can also affect this stability, phenylalanine has a bulky aromatic side group, this discards it as a stabilizer. Serine has a hydrogen bond donor or acceptor as a side chain, due to the proximity to the main chain it competes with the main chain to form NH and CO bonds. Alanine is the most common amino acid in alpha-helix structures because it has a short and no charged R group (unlike arginine that even when it's short it has a charged R-group), this makes it flexible enough to keep the structure stabilized.
Hope you find this information useful! good luck!
Answer:
amino acids
Explanation:
A protease is an enzyme capable of catalyzing the breakdown of proteins into polypeptide fragments and single amino acids, which are the building block of proteins. Proteases act by breaking peptide bonds by a process called hydrolysis, a reaction where water molecules break down peptide bonds (hydro means water and lysis means split). Proteases can be classified depending on the catalytic residue into cysteine, serine, threonine, aspartic, glutamic and metalloproteases.
