You are watching: Protein folding is a thermodynamically favorable process under physiological conditions because:
True or false: Proteins can not self-assemble right into a useful conformation after ~ they have actually been denatured.
Protein urgently is a random process, through which a vast variety of possible conformations room tested to uncover the wanted most secure state.
True or false: A prosthetic team is usually a little organic molecule compelled for activity by a protein
true or false: Proteins have actually an asymmetrical tertiary structure, when multisubunit proteins can exhibit several types of symmetry.
1) The protein crease to make itself as compact together possible.2) The packing of the protein is such that hydrophilic residues appear on the surface where lock can communicate with one aqueous environment.3) person who is abnormal of the protein"s surface permit for the development of clefts, i m sorry are regularly where the protein promotes a chemistry transformation.4) regions of secondary structures folding on one an additional are examples of the protein"s tertiary structure.
1) It entails a complicated of 2 or much more proteins interacting with every other.2) The subunits that the structure have the right to be either similar or different.3) The interactions between subunits can give rise come indefinite expansion of polymeric complexes.4) many assemblies of protein subunits have actually one or more defined axis the rotation.
True or false: Hydrophobic residues fill together due to the fact that the side chains are attracted to each various other through valve der Waals interactions
True or false: bag of α-helices twist about each other in a coiled-coil structure hosted together totally by hydrophobic interactions.
True or false: The interactions the stabilize multisubunit complexes are different to those the stabilize tertiary structure.
True or false: because that globular proteins, Hydrophobic residual water are typically on the inside and hydrophilic residues are on the outside.
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2) remove urea by dialysis and then enabling air oxidation that the denatured protein revived the protein come its original functionality.3) Denaturing the protein through both urea and β-mercaptoethanol yielded an inactive protein.4) Protein urgently is determined by its major sequence.
Fundamentals of Biochemistry: Life in ~ the molecular Level5th EditionCharlotte W. Pratt, Donald Voet, Judith G. Voet