TLS Online TPP Program

#Question id: 11405


Vulnerability to extinction can be linked to species following characteristics. Which of the following statement are correct?

A. Endemism species are more prone to extinction than fragmented

B. Species that are capable of migrating between fragments of habitat, such as between mainland areas and islands, may be more resistant to extinction

C. Population variability species are less prone to extinct

D. Species with naturally long life spans may be more likely to become extinct

#Unit 10. Ecological Principles
  1. A and B 
  2. A and C
  3. C and D 
  4. B and D
More Questions
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