Alcantara, Joshua G.

11/03/2022
BSN 1-YB-19

1. Rigor mortis is the stiffening of a corpse that occurs in the hours following death. Using
what you know about the mechanism of motor proteins, explain what causes this stiffness.
The membranes of muscle cells become more permeable to calcium ions in the final hours
of rigor mortis, and enzymes break down actin and myosin binding sites, causing secondary,
irreversible muscular flaccidity. The released calcium ions cause troponin and tropomyosin to
travel down the muscle filament, causing muscular contraction. After the muscle has contracted,
the remaining signaling neurotransmitter acetylcholine is broken down by acetylcholinesterase,
and there are no more signals from the neurological system.
The sarcoplasmic endoplasmic reticulum calcium ATPase pump, commonly known as
SERCA, prevents calcium ions from leaving the sarcoplasmic reticulum and sequesters them in
quarantine regions. There aren't enough calcium ions for myosin to move, so it can't move. Only
continuous nervous system impulses in the living organism can keep a muscle tensed for an
extended amount of time. Muscle contraction in the dead is purely the result of chemical imbalance
due to the lack of nervous system impulses. The SERCA pump consumes a large amount of ATP,
yet after death, all metabolic activity ceases and no ATP is created. This resulted in a sarcomere
with chronically elevated calcium ion levels and no way to sequester them. As a result, the SERCA
pump can't get rid of them. As a consequence, this will result in a sustained contraction or what
we called rigor mortis.

2. Globular proteins are typically constructed from several layers of secondary structure,
with a hydrophobic core and a hydrophilic surface. Is this true for a fibrous protein such as
keratin?

Fibrous proteins are elongated strand-like structures that can be viewed as rods and wire.
They play a role in structural functions such as support and protection, whereas globular proteins
play a role in metabolic processes. In regard to the amino acid sequence, keratin comprises roughly
40% hydrophilic and 60% hydrophobic chemical complexes in its structure. Because the strands
of fibrous proteins, such as keratin, are hydrogen-bonded to each other, only a few exposed groups
interact with water molecules, making them insoluble in water.

3. Straight hair can be curled and curly hair can be straightened by exposing wet hair to a
reducing agent, repositioning the hair with rollers, then exposing the hair to an oxidizing
agent. Explain how this procedure alters the shape of the hair.

Proteins, keratin, and melanin makeup hair. The shape of hair is maintained by hydrogen
molecular connections in the keratin, which can be adjusted in two ways by chemical bonding in
keratin: non-covalent hydrogen bonds and covalent disulfide bonds. Simply told, you may change
the appearance of your hair by using heat or water. Human hair has a large amount of cysteine,
which contributes to the fibers' physical qualities.When two adjacent cysteine residues join
together to form cystine, it provides a link between the two proteins, which is important for
chemical alteration of hair, especially when considering its oxidation and reduction susceptibility.
Reduced cysteine residues are transported closer to other keratin chains as reducing chemicals
break the disulfide bonds in the keratin. Disulfide bonds are produced when the sulfhydryl groups
are oxidized in the presence of an oxidizing agent. When receiving a perm for your hair, for
example, the solution contains a reducing agent with thiol compounds that breaks down disulfide
bonds by providing a hydrogen atom to each sulfur, allowing a polypeptide chain to glide into its
new shape.

4. Draw your name using peptides. Note its properties.

use the link provided. http://pepdraw.com/