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A covalent inhibitor is one that forms a stable covalent bond with an amino acid residue within the active site of an enzyme. This kind of interaction can irreversibly inhibit the enzyme's activity by blocking its active site or altering its structure. Examples include penicillin binding to serine in the active site of penicillinase.
Bromine forms a diatomic molecule, so it has a covalent bond.
A covalent bond forms between Cl and P. In this bond, the atoms share electrons to achieve a stable electron configuration.
Covalent bond.
A covalent bond forms when electrons are shared between atoms. In this type of bond, atoms share one or more pairs of electrons to achieve a stable electron configuration.
A covalent inhibitor is one that forms a stable covalent bond with an amino acid residue within the active site of an enzyme. This kind of interaction can irreversibly inhibit the enzyme's activity by blocking its active site or altering its structure. Examples include penicillin binding to serine in the active site of penicillinase.
Bromine forms a diatomic molecule, so it has a covalent bond.
Covalent bond.
A covalent bond forms between Cl and P. In this bond, the atoms share electrons to achieve a stable electron configuration.
Carbon forms covalent bond when it shared electrons with other atoms.
A compound is formed from atoms. Covalent bond is weaker.
Covalent bond.
This is a covalent bond.
The bond is covalent. If the bond is made by transferring electrons then it is an ionic bond, but if they are sharing the it is covalent.
A covalent bond forms when electrons are shared between atoms. In this type of bond, atoms share one or more pairs of electrons to achieve a stable electron configuration.
SCl2 forms a covalent bond. Sulfur and chlorine are both nonmetals, so they share electrons to form a covalent bond.
Hydrogen gas (H2) forms a nonpolar covalent bond. In this bond, the shared pair of electrons is equally shared between the two hydrogen atoms.