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liq [111]
3 years ago
8

Which are different structures of the eye? Select four options.

Chemistry
2 answers:
Setler [38]3 years ago
5 0

Answer:

Pupil, Cornea, Retina, and Lens

Explanation:

Drupady [299]3 years ago
3 0
Pupil, cornea, retina, lens
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Choose all the answers that apply.
max2010maxim [7]

Answer: has properties similar to other elements in group 18, does not react readily with other elements, is part of the noble gas group

Explanation: I’ve done on edg before

6 0
2 years ago
Calculate the vapor pressure in torr of a solution containng 24.5 g of glycerin (C3H8O3) in 135 mL water at 30.0* C; the vapor p
Otrada [13]
Psolution = X · PH_20
= 0.966 · 31.8 torr
= 30.7 torr
3 0
2 years ago
The lock-and-key model and the induced-fit model are two models of enzyme action explaining both the specificity and the catalyt
ivolga24 [154]

Answer:

The lock-and-key model:

c. Enzyme active site has a rigid structure complementary

The induced-fit model:

a. Enzyme conformation changes when it binds the substrate so the active site fits the substrate.

Common to both The lock-and-key model and The induced-fit model:

b. Substrate binds to the enzyme at the active site, forming an enzyme-substrate complex.

d. Substrate binds to the enzyme through non-covalent interactions

Explanation:

Generally, the catalytic power of enzymes are due to transient covalent bonds formed between an enzyme's catalytic functional group and a substrate as well as non-covalent interactions between substrate and enzyme which lowers the activation energy of the reaction. This applies to both the lock-and-key model as well as induced-fit mode of enzyme catalysis.

The lock and key model of enzyme catalysis and specificity proposes that enzymes are structurally complementary to their substrates such that they fit like a lock and key. This complementary nature of the enzyme and its substrates ensures that only a substrate that is complementary to the enzyme's active site can bind to it for catalysis to proceed. this is known as the specificity of an enzyme to a particular substrate.

The induced-fit mode proposes that binding of substrate to the active site of an enzyme induces conformational changes in the enzyme which better positions various functional groups on the enzyme into the proper position to catalyse the reaction.

4 0
3 years ago
How many grams of k2so4 would you need to prepare 1500 g of 5.0% k2so4 solution?
son4ous [18]
Data Given:
                                  % w/w  =  5 %

                    Solution weight  =  1500 g

                       Solute weight  =  ?

Formula Used:
                            % w/w  =  (Mass of Solute / Mass of Solution) × 100

Solving for Mass of Solute,
         
                       Mass of Solute  =  (% w/w × Mass of Solution) ÷ 100

                       Mass of Solute  =  (5 × 1500 g) ÷ 100

                       Mass of Solute  =  75 g K₂SO₄
5 0
3 years ago
2H2(g)+2NO(g)→2H2O(g)+N2(g) Part A If the concentration of NO changed from 0.100 M to 0.025 M in the first 15 minutes of the rea
andrew11 [14]

Answer:

0.0025 M/min

Explanation:

The rate of a reaction can be calculated for an element, based on its stoichiometric coefficient. For a reaction:

aA + bB = cC + dD , the rate will be

r = -(1/a)x(Δ[A]/Δt) = -(1/b)x(Δ[B]/Δt) = (1/c)x(Δ[C]/Δt) = (1/d)x(Δ[D]/Δt)

Where Δ[X] is the variation of the concentration of the X compound, Δt is the time variation, and the signal of minus in the reagents compounds is because they are disappearing, so Δ[X] will be negative, and r must be positive. So, for the reaction given:

r = -(1/2)x(Δ[NO]/Δt)

r = -(1/2)x( (0.025 - 0.1)/15)

r = 0.0025 M/min

6 0
3 years ago
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