TLS Online TPP Program

#Question id: 9273


In the higher excited state, chlorophyll is extremely unstable; it rapidly gives up some of its energy to the surroundings as heat, and enters the lowest excited state, the excited chlorophyll has four alternative pathways for disposing of its available energy: fluorescence, Heat loss, energy transfer, photochemistry; all process takes place in which wavelength,

#Unit 6. System Physiology – Plant
  1. 350-550 nm
  2. 600-700 nm
  3. 400-500 nm
  4. 700-800 nm
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TLS Online TPP Program

#Question id: 845

#Unit 1. Molecules and their Interaction Relevant to Biology

The most common cystic fibrosis– causing mutation is the deletion of a Phe residue at position____ in CFTR, which causes improper protein folding

TLS Online TPP Program

#Question id: 846

#Unit 1. Molecules and their Interaction Relevant to Biology

The maintenance of the steady-state collection of active cellular proteins required under a particular set of conditions, called ______.

TLS Online TPP Program

#Question id: 847

#Unit 1. Molecules and their Interaction Relevant to Biology

A proposed pathway for the action of E.coli chaperonins  are groEL and groES.groEL exist in trans and cis structure transferring with its bound ATP now become the cis ring once the groES  bound to it ATP hydrolysis takes place and improperly folded protein get properly folded, total number of  ATP molecules are required to per folding cycle;

TLS Online TPP Program

#Question id: 848

#Unit 1. Molecules and their Interaction Relevant to Biology

Which of the brain diseases is not caused by the misfolding of brain proteins in mammals

TLS Online TPP Program

#Question id: 849

#Unit 1. Molecules and their Interaction Relevant to Biology

The rigidity of the peptide unit and the restricted set of allowed phi and psi angles limits the number of structures accessible to the unfolded form sufficiently to allow:-

TLS Online TPP Program

#Question id: 850

#Unit 1. Molecules and their Interaction Relevant to Biology

The experimental inverse of protein structure prediction, has provided insights into protein folding and stability. Protein design attempts to construct an amino acid sequence that will form a structure such as a sandwich of β sheets or a bundle of α helices;