Indicate the statements that support the relationship between protein and struct
ID: 68802 • Letter: I
Question
Indicate the statements that support the relationship between protein and structure. A. A protein that unfolds or is incorrectly folded can use chaperones to correct the structure. B. when some proteins are denatured, with return of the normal environmental conditions they might refold. C. A proteins final shape is determined by the secondary structure. D. pH, temperature and agitation can denature proteins rendering them active. E. A disease may occur if proteins do not fold correctly. Mark for Review What's This? Question 30 of 48 3.75 Points Which statements describe sodium atoms? Select all that apply. A. outer energy level is stable B. has 2 electrons in the first energy level C. forms cations D. contains 1 valence electron E. easily forms covalent bonds F. closest to the left side of the periodic table G. can lose one electron easily Mark for Review What's This? Question 31 of 48 3.75 Points Noncompetitive inhibition occurs when A.a substance binds at the activity site B.a substance binds on a site away from the active site C.denaturing an enzyme D.increasing the activity of an enzyme Reset Selection
Explanation / Answer
A protein that unfolds or is incorrectly folded can use chaperones to correct the structure. - Correct
when some proteins are denatured, with return of the normal environmental conditions they might refold- Correct, some favourable condition could be oxidation and pH
A proteins final shape is determined by the secondary structure - True
A disease may occur if proteins do not fold correctly- Correct
pH, temperature and agitation can denature proteins rendering them active- False, as these factors can denature the protein hence will make it les active.
Sodium atom-
B.has 2 electrons in the first energy level
C. forms cations
D. contains 1 valence electron
F.closest to the left side of the periodic table
Non competetive inhibition can occur when
a substance binds on a site away from the active site