#Question id: 873
#Unit 1. Molecules and their Interaction Relevant to Biology
Intrinsically disordered proteins have properties that are distinct from classical structured proteins
A. Are characterized by sequences rich in certain polar and charged amino acids (Gln, Ser, Pro, Glu, Lys, Gly, and Ala)
B. Ordered proteins tend to participate in signaling and regulation, whereas Intrinsically disordered proteins are involved largely in catalytic reactions, transport processes, and structural functions.
C. Nearly half of all prokaryotic proteins contain long disordered segments, whereas only a few percent of eukaryotic proteins do.
D. Often adopt a specific secondary or tertiary structure when they bind to other molecules such as ions, organic molecules, proteins, and nucleic acids.
#Question id: 874
#Unit 1. Molecules and their Interaction Relevant to Biology
Fates of misfolded proteins, according given figure
#Question id: 875
#Unit 1. Molecules and their Interaction Relevant to Biology
Why positive phi angles less common than negative Phi angles in proteins contain L amino acid?
#Question id: 876
#Unit 1. Molecules and their Interaction Relevant to Biology
Prion protein is a normal constituent of brain tissue in all mammals which of the following statements are correct regarding prion protein
a) Strains of mice lacking the gene for PrP suffer no obvious ill effect
b) Illness occurs only when the normal cellular PRP or prpc occurs in an altered confirmation called PrPsc
c) The interaction of prpsc with the prpc converts the letter to prpsc initiating a Domino effect in which more and more the brain proteins converted to the disease causing form
d) the structure of prpsc is very different with much of the structure converted to amyloid like Alpha sheet.
#Question id: 877
#Unit 1. Molecules and their Interaction Relevant to Biology
The sharp transition seen in Figure suggests that
A. Proteins can be denatured by any treatment that disrupts the weak bonds stabilizing tertiary structure, such as heating, or by chemical denaturants such as urea or guanidinium chloride.
B. A comparison of the degree of unfolding as the concentration of denaturant increases reveals a sharp transition from the folded, or native, form to the unfolded, or denatured form, suggesting that only these two conformational states are present to any significant extent.
C. A similar sharp transition is observed if denaturants are removed from unfolded proteins, allowing the proteins to fold.
D. Protein folding and unfolding is an “all or none” process that results from a cooperative transition .
#Question id: 878
#Unit 1. Molecules and their Interaction Relevant to Biology
Can a peptide bind more strongly to an unfolded than the same protein in a folded state?