BIOS 255: Test 2 Questions and Answers
ATP synthase Correct Ans-- multi-enzyme complex
- 2 major subunits
mRNA transcription complex Correct Ans-about 60 proteins
- a macromolecule
Virus Correct Ans-infective molecular complexes of nucleic acid and proteins (Zika)
Denaturation Correct Ans-loss of a protein's shape
Renaturation Correct Ans-Regaining of biological activity via assembly into native 3D shape
, BIOS 255: Test 2 Questions and Answers
Native Protein Orientation Correct Ans-3D spatial orientation that is the most
thermodynamically stable & has the lowest free energy expenditure ( forms spontaneously)
Helix Correct Ans-- spiral staircase-like shape
-common protein confirmation
Fiber Correct Ans--elongated bound monomers
- common protein conformation
Globular Correct Ans--roughly a sphere
- common protein confirmation
- native confirmation for most enzymes
- hydrophobic interior pocket
- hydrophilic exterior surface
- this maximizes the number of H-bonds formed
, BIOS 255: Test 2 Questions and Answers
Physical forces that shape confirmations Correct Ans-weak electrostatic forces:
- non covalent bonds, h-bonds, hydrophobic & hydrophilic interactions, & strong covalent
bonds
Lock & Key Correct Ans-
Induced Fit Hypothesis Correct Ans-when a glucose molecule comes close to the
hexokinase active site it induces a conformational shift in the enzyme to better hold the
substrate glucose
Unstructured portion proteins Correct Ans-a protein that lacks a fixed or ordered three-
dimensional structure
- best for signaling, regulation, and control functions
, BIOS 255: Test 2 Questions and Answers
Why is there no free rotation in peptide bonds? Correct Ans-This is true because a peptide
bond is planar as are all atoms bonded to it & occur in the same plane
- restructs protein confirmation
How folding changes 3D confirmation Correct Ans-via orderly steps in a sequential way
-Steps:
First secondary, then structural motifs & assembly of complex domains, followed by tertiary
forces or quaternary shapes
Molecular Chaperons Correct Ans-Bind and stabilize newly made unfolded proteins
preventing these proteins from self aggregating and/or being denatured before folding
ATP synthase Correct Ans-- multi-enzyme complex
- 2 major subunits
mRNA transcription complex Correct Ans-about 60 proteins
- a macromolecule
Virus Correct Ans-infective molecular complexes of nucleic acid and proteins (Zika)
Denaturation Correct Ans-loss of a protein's shape
Renaturation Correct Ans-Regaining of biological activity via assembly into native 3D shape
, BIOS 255: Test 2 Questions and Answers
Native Protein Orientation Correct Ans-3D spatial orientation that is the most
thermodynamically stable & has the lowest free energy expenditure ( forms spontaneously)
Helix Correct Ans-- spiral staircase-like shape
-common protein confirmation
Fiber Correct Ans--elongated bound monomers
- common protein conformation
Globular Correct Ans--roughly a sphere
- common protein confirmation
- native confirmation for most enzymes
- hydrophobic interior pocket
- hydrophilic exterior surface
- this maximizes the number of H-bonds formed
, BIOS 255: Test 2 Questions and Answers
Physical forces that shape confirmations Correct Ans-weak electrostatic forces:
- non covalent bonds, h-bonds, hydrophobic & hydrophilic interactions, & strong covalent
bonds
Lock & Key Correct Ans-
Induced Fit Hypothesis Correct Ans-when a glucose molecule comes close to the
hexokinase active site it induces a conformational shift in the enzyme to better hold the
substrate glucose
Unstructured portion proteins Correct Ans-a protein that lacks a fixed or ordered three-
dimensional structure
- best for signaling, regulation, and control functions
, BIOS 255: Test 2 Questions and Answers
Why is there no free rotation in peptide bonds? Correct Ans-This is true because a peptide
bond is planar as are all atoms bonded to it & occur in the same plane
- restructs protein confirmation
How folding changes 3D confirmation Correct Ans-via orderly steps in a sequential way
-Steps:
First secondary, then structural motifs & assembly of complex domains, followed by tertiary
forces or quaternary shapes
Molecular Chaperons Correct Ans-Bind and stabilize newly made unfolded proteins
preventing these proteins from self aggregating and/or being denatured before folding
