Multiple choices (one best answer for each question, 3 p each) Which of the foll
ID: 1008631 • Letter: M
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Multiple choices (one best answer for each question, 3 p each) Which of the following statements about protein-ligand binding is correct? The K_a is equal to the concentration of ligand when all of the binding sites are occupied. The K_a is independent of such conditions as salt concentration and pH. The larger the K_a (association constant), the lower the affinity. The larger the K_a, the faster is the binding. The larger the K_a, the smaller the K_d (dissociation constant). An allosteric effect of regulator to and an enzyme is binding of a regulator affects the binding the substrate binding of substrate affect the binding of protein to a regulator binding of regulator affect the catalytic property of the enzyme covalent binding of regulator affect the binding of substrate binding of regulator affect covalent catalytic property of enzyme In hemoglobin, the transition from T state to R state (low to high affinity) is triggered by: Fe^2+ binding to hemoglobin H^+ binding to hemoglobin O_2 binding to hemoglobin H_2 O binding to hemoglobin CO_2 binding to hemoglobin Which of the following is nor correct concerning cooperative binding of a ligand to a protein? It is usually a form of allosteric interaction. It usually occurs with proteins with multiple subunits. It rarely occurs in enzymes. It results in a nonlinear Hill Plot. It results in a sigmoidal binding curve.Explanation / Answer
Which of the following statements about protein-ligand binding is correct?
A) The Ka is equal to the concentration of ligand when all of the binding sites are occupied.
B) The Ka is independent of such conditions as salt concentration and pH.
C) The larger the Ka (association constant), the weaker the affinity.
D) The larger the Ka, the faster is the binding.
E) The larger the Ka, the smaller the Kd (dissociation constant).------------answer
2 An allostenc effect of regulator to and an enzyme is
A) binding of a regulator affects the binding the substrate
B) binding of substrate affect the binding of protein to a regulator).------------answer
rC) binding of regulator affect the catalytic property of the enzyme
0) covalent binding of regulator affect the binding of substrate
E) binding of regulator affect covalent catalytic property of enzyme
3. In hemoglobin, the transition from T state to R state (low to high affinity) is triggered by:
A) Fe'" binding to haemoglobin
B) *Minding to hemoglobin
C) 02 binding to hemoglobin ).------------answer
D) 14:0 binding to hemoglobin
E) CO2 binding to hemoglobin
4. Which of the following is not correct concerning cooperative binding of a ligand to a protein?
A) It is usually a form of allosteric interaction
. B) It usually occurs with proteins with multiple subunits.
C) it rarely occurs in enzymes. ).------------answer
D) It results in a nonlinear Hill Plot.
E) It results in a sigmoidal binding curve.
In natural chemistry and pharmacology, a ligand is a substance that structures a complex with a biomolecule to fill an organic need. In protein-ligand official, the ligand is normally an atom which delivers a sign by authoritative to a site on an objective protein. The coupling commonly brings about a change of adaptation of the objective protein. In DNA-ligand restricting studies, the ligand can be a little atom, ion, or protein which ties to the DNA twofold helix. The relationship amongst ligand and restricting accomplice is an element of charge, hydrophobicity, and sub-atomic structure. The case of restricting happens over a little scope of time and space, so the rate steady is typically a little number.
Restricting happens by intermolecular strengths, for example, ionic bonds, hydrogen bonds and Van der Waals powers. The relationship of docking is really reversible through separation. Quantifiably irreversible covalent holding between a ligand and target atom is atypical in organic frameworks. Rather than the meaning of ligand in metalorganic and inorganic science, in organic chemistry it is uncertain whether the ligand for the most part ties at a metal site, similar to the case in hemoglobin. All in all, the elucidation of ligand is logical concerning what kind of restricting has been watched. The historical background comes from ligare, which signifies 'to tie'.
Ligand authoritative to a receptor protein adjusts the compound adaptation by influencing the three-dimensional shape introduction. The compliance of a receptor protein creates the useful state. Ligands incorporate substrates, inhibitors, activators, and neurotransmitters. The rate of restricting is called liking, and this estimation exemplifies a propensity or quality of the impact. Restricting proclivity is realized by host-visitor communications, as well as by dissolvable impacts that can play a predominant, steric part which drives non-covalent authoritative in solution. The dissolvable gives a concoction situation to the ligand and receptor to adjust, and in this manner acknowledge or dismiss each different as accomplices.
The association of most ligands with their coupling locales can be described as far as a coupling liking. When all is said in done, high-partiality ligand restricting results from more noteworthy intermolecular power between the ligand and its receptor while low-fondness ligand restricting includes less intermolecular power between the ligand and its receptor. When all is said in done, high-partiality restricting includes a more drawn out living arrangement time for the ligand at its receptor restricting site than is the situation for low-liking official. High-partiality authoritative of ligands to receptors is frequently physiologically critical when a portion of the coupling vitality can be utilized to bring about a conformational change in the receptor, bringing about adjusted conduct of a related particle channel or chemical. ligand that can tie to a receptor, adjust the capacity of the receptor, and trigger a physiological reaction is called an agonist for that receptor.
Agonist authoritative to a receptor can be portrayed both as far as how much physiological reaction can be activated and as far as the centralization of the agonist that is required to create the physiological reaction. High-partiality ligand restricting suggests that a generally low convergence of a ligand is sufficient to maximally possess a ligand-restricting site and trigger a physiological reaction. The lower the Ki level is, the more probable there will be a substance response between the pending particle and the open antigen.
Low-partiality official (high Ki level) infers that a generally high centralization of a ligand is required before the coupling site is maximally possessed and the greatest physiological reaction to the ligand is accomplished. In the illustration appeared to one side, two distinct ligands tie to the same receptor restricting site
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