Final answer:
The false statement is Option B, which incorrectly describes the effects enzyme inhibition has on Vmax and Km. Enzyme inhibition can decrease Vmax, increase Km, or affect both, contrary to the statement which suggests it only changes one parameter.
Step-by-step explanation:
The student's question pertains to identifying the false statement among given options regarding peptide bonds, enzyme inhibition, membrane proteins, and the second law of thermodynamics as they relate to protein structure and function. Upon analyzing the statements given, we should take into account that peptide bonds are indeed covalent bonds that link amino acids together to form proteins. However, peptide bonds are not the only covalent bonds in proteins; disulfide bonds also play an essential role in stabilizing protein structure, particularly in the tertiary structure. Enzyme inhibition can affect the maximum reaction velocity (Vmax) or the Michaelis constant (Km), which indicates the substrate concentration at which the reaction rate is half of Vmax. However, inhibiting an enzyme could either decrease Vmax or increase Km, not necessarily only one as the statement B suggests. Additionally, many membrane-bound proteins indeed have alpha helices comprised of nonpolar amino acids that span the membrane. Lastly, while cells create order within their boundaries, they do so by increasing entropy elsewhere, hence complying with the second law of thermodynamics.
Considering all these pieces of information, the false statement is Option B: Inhibition of an enzyme either decreases Km or increases Vmax. Instead, enzyme inhibition can either decrease Vmax or increase Km, or affect both parameters depending on the type of inhibition.