From a thermodynamic point of view, how does a protein fold into its native and functional structure?
Answer ----->
Protein folding is driven entirely by entropy.water plays a large role in protein folding. In unfolded protein water is ordered and polypeptide chain is disordered but during folding the release of disordered water upon aggregation causes an increase in entropy .
In fact, hydrophobic domains of a protein constrain the possible configurations of surrounding water and so their burial upon folding increases the water’s entropy. Moreover, it turns out that the hydrogen bonding of polar residues and the backbone is satisfied both in an unfolded state (by water) and in a folded state (by each other). Therefore enthalpy is “zero sum,” and protein folding is driven almost entirely by entropy.
From a thermodynamic point of view, how does a protein fold into its native and functional struct...
From a thermodynamic point of view, how does a protein fold into its native and functional structure?
Protein S will fold into its native conformation only when protein Q is also present in the solution. However, protein Q can fold into its native conformation without protein S. What is the most likely explanation. Briefly explain in 1-4 sentences.
a) What aspects of protein structure and folding are explained by entropy? How does entropy affect a protein’s native versus denatured structure? b) What aspects of protein structure and folding are explained by enthalpy? How does enthalpy affect a protein’s native versus denatured structure? c) What aspects of protein structure and folding are illustrative of equilibrium (or disequilibrium)? 1. The figure below shows the physical representation of a native protein versus a denatured protein 72 native state A-state 23 17...
The terms motif (fold) and domain describe levels of protein organization more complicated than primary or secondary structure. Differentiate between motifs and domains by matching each phrase to the appropriate term. Motifs Domains Both Answer Bank clusters of secondary structure may retain a three-dimensional structure when separated from the rest of the protein Baß unit stable, globular units unit of tertiary structure depends on primary structure may be distinct functional units in a protein stabilized by hydrophobic interactions repetitive supersecondary...
Protein Folding - a) what is the molten globule? b) How does the activity of chaperones in unfolding molten globules may enhance the overall rate of folding to the native state? c) Name a protein folding disease. d) Give two possible general causes for disease arising from protein folding defects.
2. (6 points) A wild-type protein was tested for its ability to fold under several concentrations of denaturant. Two mutants of this protein were made by making a one residue substitution and then also tested under similar conditions as the wild-type. Given the two curves below, interpret how the changed residue in mutant 1 and mutant 2 affect the protein folding nucleus. Assume Kapp is measured in s-1 in Kapp in Kap [denaturant [denaturant]
2. (6 points) A wild-type protein was tested for its ability to fold under several concentrations of denaturant. Two mutants of this protein were made by making a one residue substitution and then also tested under similar conditions as the wild-type. Given the two curves below, interpret how the changed residue in mutant 1 and mutant 2 affect the protein folding nucleus. Assume Kapp is measured in s-1 Wt Muut in Kapp in Kapp [denaturant [denaturant]
A newly formed protein usually folds into its native state rapidly even before it is completely built by the ribosome. The free energy for the folding process has at least two key components-one enthalpic and the other entropic. Which of the following is/are part of the enthalpic changes that accompany protein folding? OA. Hydroxylation of prolines and lysines. B. Formation of a salt bridge between a lysine side chain and an aspartic acid side chain within the interior of the...
How does a protein suspension incorporate air? From what you know about the structure of the protein utilized, explain why some proteins performed better than others under any set of conditions you select. Did good overrun always coincide with good stability? Why or why not?
Lac I ( Gene)- non functional cannot bind the inducer How does it affect in the presence of lactose? How does it affect in absence of lactose? Lac Z( protein)- Wipeout mutation How does it affect in the presence of lactose? How does it affect in absence of lactose?