How can a cell gain energy while folding proteins in the periplasm?
The periplasmic chaperon found to be different from cytoplasmic chaperone. periplasm is devoid of ATP which generally required for proper folding conformations achieved by the proteins. There are two proteins required for the protein folding that are protein disulphide isomerases (Dsb proteins), which catalyse disulfide-bond formation, and peptidyl-prolyl isomerases (PPIase), which catalyse cis-trans isomerization of peptidyl bonds.
The maintanence of thiol isomerase's in reduced state is the rate limiting step which in turn energised by thioredoxin/thioredoxin reductase system in the cytoplasm as a source of reducing equivalents.
Why metallothioneins, a group of metallo proteins can have different folding configurations without assistance to fold into them?
The folding of proteins is thermodynamically spontaneous. a. What does this mean? How is it defined? b. This spontaneity appears, on the surface, to be counterintuitive, because of the change in entropy, going from one state to another. Explain briefly. c. How is the apparent contradiction in part (b) overcome to ensure the spontaneity of the process?
QUESTION 1 To study how proteins fold, scientists must be able to purify the protein of interest, use solvents like urea to denature the folded protein, and observe the process of refolding at successive time points. What is the effect of the solvents used in the denaturation process? a. The solvents break all noncovalent interactions. b. The solvents break all covalent interactions. c. The solvents create a new folded conformation. d. The solvents break some of the noncovalent interactions, resulting...
How can I restate "some code for proteins while some code for RNAs and contain various regulatory elements"? Can you please rephrase this sentence: "Some code for proteins while some code for mRNAs and contain various regulatory elements"? It is speaking of genes.
I 20. What are the intermolecular forces responsible for the folding of amino acid chains into proteins? Give specifics. 21. How can two different proteins have the same molecular formula, yet have different folds and structures.
EVOLUTION AND MOLECULES OF THE CELL What is the proposed pathway for the evolution of cells, and how is it explained by the endosymbiont theory? What are the major macromolecules of the cell? What are the basic characteristics of polysaccharides, lipids, nucleic acids and proteins and how do these characteristics relate to the function of these macromolecules within the cell? How do the side chains of amino acids in proteins influence protein folding and its ultimate shape?
Embedded cell membrane proteins are some of the most important proteins a cell produces. An important disease involves the malfuction of one of these proteins. This disease causes green slime to accumulate in the lungs and digestive system, leading to malnutrition and frequent pneumonias. What is the name of this disease? Cystic fibrosis Neurofibromatosis Pancreatitis Alzheimer's disease Name the high energy yield process that degrades lipids in peroxisomes. Beta-oxidation cycle Lactic acid fermentation Citric acid cycle e Dehydrogenation D Question...
1. How can protein folding affect protein function? 2. How can amino acid sequence affect protein function? 3. How can an amino acid sequence (primary sequence) dictate 3D protein structure?
Explain the thermodynamics of protein folding including in your discussion how enthalpy and entropy drive protein folding and the relative strength of its change in free energy.
How does a cell regulate location of proteins? Explain 4 specific examples.