old exam 1 Flashcards
O2 binding triggers a conformational change in hemoglobin (T/F)
True
Positive Cooperativity is when the first binding event increases affinity at remaining sites (T/F)
True - hemoglobin triggers change
Negative cooperativity is when the first binding event reduces aaffinity at remaining sites (T/F)
True - decreases the strength and closes the binding site for something else
CO2 is toxic to humans because
It binds to Fe atom in hemoglobin and prevents binding of O2
The lock and key model describes conformational changes in both the protein and the ligand when the ligand binds to the protein (T/F)
False - certain things can bind to certain proteins
beta sheet is quaternary structure (T/F)
False - its secondary
Proteins can be denatured by extremes of pH (T/F)
True
Independently stable part of a protein is called a domain (T/F)
True
O2 dissolves easily in water (T/F)
False
Anfinsens ribonuclease refolding experiment showed that the amino acid sequence determines the native confirmation (T/F)
True
In globular protein would Pro and Gly be found more in Beta or alpha
Beta turn
Calculate pH pf a solution of weak acid when molar ratio of proton acceptor to donor is 100:1 and pKa is 4.
pH= 6
Long range strong interactions between permanently charged groups
electrostatic interactions
a leucine sidechain interacting with a valine sidechain in the protein interior
hydrophobic effect
interaction of N-H and C–O of the peptide bond leads to local regular structures such as alpha and beta
hydrogen bonds