Answer:
The human eye is the prime organ of the body, which associates with the photons of light and allows one to see various things. The unique cells found in retina, which does activity of seeing are cones and rods cells. Rods help to see in dim light vision, while on the other hand, cone cells are unique in recognizing different colors.
These cells comprise photoreceptor proteins that help in trapping photons at particular wavelength. Mutation in the gene encrypting for these proteins results in permanent or temporary vision issues. The extremity of defects relies upon the degree to which mutation takes place.
The mutation in rod cells photoreceptor proteins leads to night blindness and retinitis pigmentosa. Retinitis pigmentosa refers to an inherited disorder that takes place because of early loss of rod cell, which destructs retina. On the other hand, night blindness does not mean complete blindness night, however, inadequate tendency to see in low light.
Identically, the mutation in the cone cell also results in vision issues, known as red color blindness and tritanopia. Tritanopia refers to a kind of color blindness, which originates because of insensitivity of blue receiving protein gene towards blue light. On the other hand, red color blindness refers to insensitivity of red receiving cone cells in captivating long-wavelength photons.
Answer: Protein folding and oligomerization
Explanation:
Binding immunoglobulin protein (BiP) is a vital protein present in humans essential for the translocation of secreted peptides.
BiP is a molecular chaperone which is present in lumen of ER (endoplasmic reticulum) which binds to the new protein and then translocat into the ER. The protein in ER is maintained under subsequent condition and important for protein folding and oligomerization (conversion of a monomer or group of monomer into an oligomer).
Several other functions of BiP are:
- ER translocation
- ER-associated degradation (ERAD)
- UPR pathway
Hence, BiP is a chaperone, it is important for protein folding and oligomerization.
Answer:
The elements in increasing order of atomic radius: oxygen, carbon, aluminum, potassium
Explanation:
The distance from the center of the nucleus to the outermost shell of the electron is known as the atomic radius of an element. The atomic radius decreases rightward along each period (row) of the table due to the increase in effective nuclear charge (the charge of the nucleus equal to the number of protons). Across a period, electrons are added to the same energy level and the increasing number of protons causes the nucleus to exert more pull on these electrons, which makes the atomic radius smaller. Atomic radius increases down each group (column) of the periodic table because of the addition of electrons to higher energy levels, which are further away from the nucleus and the pull of nucleus weakens. Another reason for the increase in atomic radius is the electron shielding effect, which is the reduction of the attractive force between a nucleus and its outer electrons due to the blocking effect of inner electrons
While moving from left to right in the second period, c
arbon comes before oxygen and so oxygen will have a smaller atomic radius than carbon. While moving down the periodic table, al
uminum comes before potassium even if they are not in the same period. So aluminum
's atomic radius will be smaller than that of potassium but bigger than that of carbon and oxygen.
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<span> They can be classified according to the core structural functional groups' locations as </span><span>alpha- (α-), beta- (β-), gamma- (γ-) or delta-(δ-)</span><span> amino acids; other categories relate to </span>polarity<span>, </span>pH<span> level, and side-chain group type (</span>aliphatic<span>, </span>acyclic<span>, </span>aromatic, containing hydroxyl orsulfur<span>, etc.). In the form of </span>proteins<span>, amino acids comprise the second-largest component (water is the largest) of human </span>muscles<span>, </span>cells<span> and other </span>tissues.[5]<span> Outside proteins, amino acids perform critical roles in processes such as </span>neurotransmitter<span> transport and </span>biosynthesis<span>.</span>
