TLS Online TPP Program

#Question id: 11464


Green fluorescent protein consists of a chain of 238 amino acid residues. The light-emitting group is a derivative of three consecutive amino acids are

#Unit 1. Molecules and their Interaction Relevant to Biology
  1. Trp, Tyr, and Gly
  2. Ser, Tyr, and Lys
  3. Ser, Val and Gly
  4. Ser, Tyr, and Gly
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TLS Online TPP Program

#Question id: 11926

#Unit 9. Diversity of Life Forms

The chloroplasts of all of the following are derived from ancestral red algae, except those of

TLS Online TPP Program

#Question id: 20967

#Unit 12. Applied Biology

Transgenic models exist for ________ disease.

TLS Online TPP Program

#Question id: 182

#Unit 1. Molecules and their Interaction Relevant to Biology

Which amino acid is least likely to participate in acid-base catalysis?

TLS Online TPP Program

#Question id: 1324

#Unit 4. Cell Communication and Cell Signaling

What are the two major proteins that comprise tight junctions?

TLS Online TPP Program

#Question id: 879

#Unit 1. Molecules and their Interaction Relevant to Biology

 Correct approaches to protein structure prediction-:

i. Homology modeling

a) Methods is the Rosetta program, formulated by David Baker. To satisfy the program’s computational needs, a volunteer network of ∼100,000 computers, known as Rosetta@home, provides the 500,000 or so hours of processing time required to generate a structure.

ii. Structural genomics

b) which seeks to determine the X-ray structures of all representative domains, is aimed at expanding this predictive technique. The identification of structural homology is likely to provide clues as to a protein’s function even with imperfect structure prediction.

iii. Threading

c) Is a computational technique that attempts to determine the unknown structure of a protein by ascertaining whether it is consistent with a known protein structure. It does so by placing the unknown protein’s residues along the backbone of a known protein structure and then determining whether the amino acid side chains of the unknown protein are stable in that arrangement

iv. Ab initio

d) Aligns the sequence of interest with the sequence of a homologous protein or domain of known structure—compensating for amino acid substitutions, insertions, and deletions—through modeling and energy minimization calculations.