To answer this question, we must first look at the
reactivity series table. From the table, we can see that those which are
located above are the most reactive while those below are less reactive. Which
means that elements cannot replace those elements which are above them.
From the series, platinum is below lead, hence there will
be no reaction.
Answer:
No reaction
answer is atom.Hope it is helpful.
As mentioned above, phosphoric acid has 3 pKa values, and after 3 ionization it gives 3 types of ions at different pKa values:
H₃PO₄(aq)
+ H₂O(l) ⇌ H₃O⁺(aq) + H₂PO₄⁻ (aq) pKₐ₁
<span>
</span>H₂PO₄⁻(aq) + H₂O(l) ⇌ H₃O⁺(aq) + HPO₄²⁻ (aq) pKₐ₂
HPO₄²⁻(aq) + H₂O(l) ⇌ H₃O⁺(aq) + PO₄³⁻ (aq) pKₐ₃
At the highest pKa value (12.4) of phosphoric acid, the last OH group will lose its hydrogen. On the picture I attached, it is shown required protonated form of phosphoric acid before reaction whose pKa value is 12.4.
Answer:
Scientists seek to eliminate all forms of bias from their research. However, all scientists also make assumptions of a non-empirical nature about topics such as causality, determinism and reductionism when conducting research. Here, we argue that since these 'philosophical biases' cannot be avoided, they need to be debated critically by scientists and philosophers of science.
Explanation:
Scientists are keen to avoid bias of any kind because they threaten scientific ideals such as objectivity, transparency and rationality. The scientific community has made substantial efforts to detect, explicate and critically examine different types of biases (Sackett, 1979; Ioannidis, 2005; Ioannidis, 2018; Macleod et al., 2015). One example of this is the catalogue of all the biases that affect medical evidence compiled by the Centre for Evidence Based Medicine at Oxford University (catalogueofbias.org). Such awareness is commonly seen as a crucial step towards making science objective, transparent and free from bias.
Answer:
Michaelis constant is known as km which is the substrate concentration that encourages the compound to work at half maximum velocity represented by Vmax/2. Michaelis constant is inversely related to the substrate and the affinity of the enzyme.
Induced fit model: The premise of the purported induced fit hypothesis, which expresses that the attachment or association of a substrate or some other atom to an enzyme causes an adjustment to the enzyme in order to fit or restrain its activity.
In substrate, analog Km or Michaelis constant will be high as the substrate will stay because of analogs inhibit activity.
In the transitional state, analog Km will be in the middle of the substrate and product analogs. Progress state analogs are synthetic mixes with a structure catalyzed reaction that looks like the progressing condition of a substrate atom in a compound enzyme.
In item simple thus Km is the least.
0.0013 M = product ananlog,
0.025 M=Transition state, and
0.0045 M = Substrate analog
