You can't calculate the electronegativity difference of a single molecule you'll need a frame of reference to explain the electronegativity difference and properties arising due to the difference. Another term arise here is modified electronegativity that is calculated within the molecule between two atoms of different electronegativity and use to explain the nature of molecule wether they are electron withdrawing group or electron donating group and also used to compare the electronegativity with other molecule!
Answer:
In a chemical reaction the total mass of all the substances taking part in the reaction remains the same. ... The law of conservation of mass states that the total mass of substances taking part in a chemical reaction is conserved during the reaction.
Explanation:
Answer: A polar bond is a covalent bond between two atoms where the electrons forming the bond are unequally distributed.
Example: A water molecule, abbreviated as H2O, is an example of a polar covalent bond. The electrons are unequally shared, with the oxygen atom spending more time with electrons than the hydrogen atoms.
They form a covalent bond
Answer:
D. The side chains of D-Arg and D-Lys are not positioned to bind correctly at the active site
Explanation:
Stereospecificity is the ability to distinguish between stereoisomers of of a particular compound. L- and D- structures of compounds in living organisms are usually present in only one form due to stereospecificity. For example, naturally occuring amino acids in proteins are usually present as L-isomers.
Since enzyme are proteins, their active sites are composed of L-amino acid and they show stereospecificity in the reactions they catalyze. In their binding sites, only substrates complementary in structure can bind in order for catalysis to proceed. Therefore, only amino acids in the L- configuration are complementary to the active site of enzymes.
In the case of serine proteases, The side chains of -Arg and D-Lys will not be positioned properly for binding at the binding site of serine proteases, therefore, no catalysis will occur. On the other hand, L-Arg and L-Lys can bind to the catalytic site of serine proteases since they are complementary fits to the active site of the enzymes.