TLS Online TPP Program

#Question id: 11129


Which of the following statements concerning the neuronal membrane at rest is correct?

#Unit 7. System Physiology – Animal
  1. The extracellular sodium concentration is less than its intracellular concentration
  2. The concentration of chloride is greatest inside the cell
  3. If the resting potential is moved to a more negative value, the cell becomes more excitable
  4. The concentration gradient for potassium is such that it tends to move out of the cell
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TLS Online TPP Program

#Question id: 23752

#Unit 1. Molecules and their Interaction Relevant to Biology

Which one of the following is always associated with a 'tree'?

TLS Online TPP Program

#Question id: 23751

#Unit 1. Molecules and their Interaction Relevant to Biology

Which one of the following is always associated with 'Justice'?

TLS Online TPP Program

#Question id: 703

#Unit 1. Molecules and their Interaction Relevant to Biology

Which of the following statements concerning protein domains is true?

TLS Online TPP Program

#Question id: 913

#Unit 1. Molecules and their Interaction Relevant to Biology

The appropriate folding of a newly translated product is essential, and continual misfolding often leads to disease, especially in vertebrates. This misfolding, particularly in the situation of prion diseases, may be due to

TLS Online TPP Program

#Question id: 912

#Unit 1. Molecules and their Interaction Relevant to Biology

Which of the following is correct about the native state of a protein

a. is unaffected by changes in temperature and pH.

b. corresponds to the highest Gibbs free energy state.

c. is determined by its primary amino acid sequence.

d. corresponds to the lowest entropic state.

TLS Online TPP Program

#Question id: 911

#Unit 1. Molecules and their Interaction Relevant to Biology

The correct order for molecular chaperone–mediated protein folding is:

I – exchange of ATP for ADP on chaperone

II – chaperone undergoes conformational change, which affects protein folding

III – chaperone binds to exposed hydrophobic residues on unfolded protein

IV – folded protein is released