#Question id: 23112
#Unit 2. Cellular Organization
#Question id: 28465
#Unit 5. Developmental Biology
Optic vesicle secrete two paracrine factor for the lens formation these signalling factor known as___
#Question id: 7248
#Unit 5. Developmental Biology
Planning of the Xenopus mesoderm along the dorso-ventral axis contains an antagonistic relationship between chordin and bmp-4. Is there an analogy here to dorso-ventral patterning in the Drosophila embryo?
#Question id: 1220
#Unit 4. Cell Communication and Cell Signaling
Many G protein-coupled receptors contain seven transmembrane α-helical domains. The amino end of the protein lies at the exterior of the plasma membrane. Loops of amino acids connect the helices either at the exterior surface or on the cytosolic surface of the membrane. The loop on the cytosolic side between helices 5 and 6 is usually substantially longer than the others. Where would a coupled G protein most likely interact with this receptor?
#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. |