1) How does Hsp70-mediate correct protein folding?

2) How do Hsp70-like proteins affect existing interactions between proteins?

3) How does Hsp60 enable protein re-folding?

-Be able to explain the mechanisms for these, including usage of ATP, etc.

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Elin HesselLv2

9 May 2019

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Related questions

1. Enzyme A is an enzyme that catalyzes the reaction of glucose + fructose to sucrose by coupling this +âG reaction with the -âG hydrolysis of ATP. A chemical is discovered that keeps Enzyme A from entering its transition state. What will happen when this enzyme is added to a solution containing ATP and equal parts of glucose, fructose, and sucrose?

A. All of the glucose + fructose will be converted to sucrose.

B. All of the sucrose will be converted to glucose + sucrose.

C. The glucose + fructose will reach their equilibrium constant with sucrose.

D. The ATP will phosphorylate the glucose to produce sucrose while leaving fructose.

2.Which of the following does not contribute to how an individual protein functions?

A. sequence of amino acids.

B. The quaternary structure of that protein.

C. The shape of the binding site.

D. The number and position of charged and polar amino acids.

3. In order to perform functions that proteins alone cannot do, proteins can:

A. Incorporate other molecules into their structure.

B. bind to other proteins to form a complex.

C. signal to non-protein enzymes to perform the function.

D. undergo a conformational change to perform the function.

4. Which of the following is not a function of intrinsically disordered sequences in a protein?

	A. Acting as substrates for chemical interactions.
	B. Increasing variation in a protein by swapping amino acids.
	C. Providing elasticity to tissues.
	D. Flexing to enable interactions between domains.

1. The phospholipid bilayer is about 5 nm thick (from polar head of one leaflet to polar head of the other leaflet). A water molecule has a diameter of about 4 Ã . How many water molecules could line up along a protein channel that spans the membrane, end to end?

2.Describe or identify the differences between Gram-negative and Gram-positive bacteria with respect to their envelope / wall structures. How do the antibiotics, penicillin and ampicillin, prevent bacterial growth?

3. A mutant protein functions at a cool temperature such as 25ÂºC but not at 37ÂºC. What is likely happening to the protein at the warmer temperature? Think of the role of noncovalent interactions protein folding and in protein-protein interactions.

4. State and explain the first two laws of thermodynamics. Which of the two laws predicts the spontaneity of a particular reaction? How is it that organisms, through various syntheses, do not defy the second law of thermodynamics?

Thank you, xoxo

maroonarmadillo93

1. How can we make anantibody to a specific protein?

2. In what ways can thisantibody be used as a molecular tool in studying thisprotein?

3. Explain the differencebetween an allosteric and competitive inhibitor.

4. What are the fourlevels of protein organization? Explain them.

5. In SDS-Page, proteinsare separated by length. If the same length proteins can fold intoloose (bigger) or condensed (smaller) shapes and can even complexwith other proteins, how are individual proteins separated solelyaccording to their length? Additionally, proteins can havedifferent charges. Proteins with more basic amino acids have agreater negative charge while proteins with more acidic amino acidshave a greater positive charge. Proteins travel from the negativeelectrode to positive electrode in SDS-Page. How does theirintrinsic charge not affect their migration (true for mostproteins)?