Answer:
the enzyme and substrate fit together like a lock and key.
Answer:
(C) Aminoacyl-tRNA synthetases have an additional active site that binds to non-cognate tRNAs. The tRNAs that bind to this second active are hydrolyzed and released from the enzyme.
Explanation:
In case of translation, proof reading is done by aminoacyl-tRNA synthetases only. Aminoacyl-tRNA synthetases have two mechanisms to avoid error during translation which are mentioned as under:
<u>(1) Chemical proof reading:</u> Incorrect amino acids rather than being hydrolyzed in catalytic pocket get hydrolyzed in editing pocket and thus they hardly get attached to tRNA.
For example: For distinguishing similar amino acids like isoleucine and valine, isoleucyl-tRNA synthetase uses a second active site which is meant for only valine not for isoleucine. In this particular site, valine which had entered the enzyme is cleaved away with the help of editing reaction after which the enzyme is well prepared to process isoleucine which is the correct amino acid for this enzyme.
<u>(2) Kinetic proof reading: </u>Even if an incorrect amino acid has entered a particular aminoacyl-tRNA synthetase, it does not cause appropriate conformational change in the enzyme because of which the incorrect amino acid loosens from the enzyme and does not get incorporated.
Note: In this example, only chemical proof reading is mentioned not kinetic proof reading.
Answer:
8
Explanation:
What is the number of white blood cells permitted in a unit of leukoreduced red cells? 8 g/dL owing to chemotherapy with a drug known to cause bone marrow depression and immunodeficiency.
The statement that best describes the work of these researchers is "As a result, the researchers have been able to achieve protein-folding simulations that are far better than those other computing methods have done." I hope my answer has come to your help. God bless and have a nice day ahead!
