BIO 360 Lecture Notes - Lecture 6: Dissociation Constant, Hydrophile

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15 Aug 2022

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Functions / examples: storage of tons / molecules (cid:8869) myoglobin , ferritin. 2. transport 10ns / molecules (cid:8869)hemoglobin , serotonin transporter: defense against pathogens (cid:8869) antibodies , cytokines, muscle contraction (cid:8869) actin, myosin, biological catalysts (cid:8869) chymotrypsin ,lysozyme keys to function, reversible binding of ligands, specific ligands / binding sites. 3. induced fit - ligand binding (conformational /dramatic changes: cooperatively- multi subunit proteins (conformational changes in one subunit that affects others, regulated interactions (cid:8869) a-+ b. Reversible transient process of equilibrium protein - ligand binding interaction basics. Ligand binds -10 same non covalent interactions dictating protein structure. Binding site region in protein that binds ligands (cid:8869) typically small. Specificity : lock - and - key model proteins high specificity (cid:8869)explained by complementary of the binding site / ligand. Complementary in : (cid:8869) size, shape, charge, hydrophobic/ hydrophilic. Lock and key model by emil fisher ( 1894) complementary surfaces are performed.

Related Questions

Hemoglobin is a protein that binds oxygen and represents a well-characterized example of allosteric ligand binding. It undergoes a concerted conformational change between T- and R-states upon oxygen binding and displays strong positive cooperativity upon ligand binding (indicates that the affinities for binding the 1^st, 2^nd, 3^rd, and 4^th ligands are not equivalent). Please choose the statement below that best describes hemoglobin as related to the topic of allostery.â

A. The binding of oxygen by hemoglobin is described by a hybrid model of allostery that blends features of the MWC and KNF models

B. The binding of oxygen by hemoglobin is not described as an allosteric process

C. Hemoglobin adheres strictly to the KNF (sequential) model of allostery due to the observation of strong positive cooperativity

1) How do hydrophobic clustering forces affect binding between molecules?

- i.e. protein-protein interactions, or binding of a small molecule to a protein

2) How is binding specificity between molecules controlled?

- what makes it possible for proteins bind to a specific target?

1. Which non-covalent interaction is primarily
responsible for stabilizing a helices, Ã sheets, and Ã
turns?
a. Hydrophobic interactions.
b. Ion-pairing.
c. Hydrogen bonding.
d. Stacking of aromatic rings.
e. Van der Waals interactions.

2.Which is not associated with the formation of oligomers?
a. Increased stability compared to the dissociated subunits.
b. The formation of active sites between adjacent subunits.
c. Contact between the subunits that allows for changes in
quaternary structure when ligands bind. This can control
biological activity.
d. Increased efficiency by synthesizing smaller subunits
rather than a single chain the same size as the oligomer.
e. An enhanced ability to adopt F and ? angles outside the
common ranges.

3. Would you expect myoglobin that is injected
intravenously to perform the same function as
hemoglobin? Explain.
a. No, myoglobin cannot release oxygen as well to the
tissues.
b. No, because the heme of myoglobin binds oxygen at a
different coordination site.
c. No, because 2,3-BPG completely inhibits the binding of
oxygen to myoglobin.
d. Yes, in the blood myoglobin adopts a similar quaternary
structure as hemoglobin and binds oxygen with positive
cooperativity.
e. Yes, because both bind oxygen very easily in the lungs.

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BIO 360 Lecture Notes - Lecture 6: Dissociation Constant, Hydrophile

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