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First Aid: Biochemistry Molecular

Instructions:
  • Answer 50 questions in 15 minutes.
  • If you are not ready to take this test, you can study here.
  • Match each statement with the correct term.
  • Don't refresh. All questions and answers are randomly picked and ordered every time you load a test.

This is a study tool. The 3 wrong answers for each question are randomly chosen from answers to other questions. So, you might find at times the answers obvious, but you will see it re-enforces your understanding as you take the test each time.
1. Three amino acids necessary for purine synthesis= glutamine - aspartate and glycine






2. Condensed - transciptionally inactive HC- Highly condensed






3. Rampant - Massive - TIny rRNA is most common - then mRNA and then tRNA






4. AD and AR- associated iwth joint dislocation - berry aneurysms - organ rupture






5. Responsible for the accuracy of amino acid selection






6. Change resulting in early stop codon






7. A site - incoming aminoacyl tRNA - Psite accomodates growing Peptide - E site holds EmplytRNA as it exits






8. Site where negative regulators bind






9. Aminoacyl - tRNA binds to A site 2) peptidyltransferase catalyzes peptide bond formation transfers growing polypeptie to amino acid in A site 3) ribosome advances 3 nucleotides toward the 3 prime end of RNA moving peptiydyl RNA to P site






10. Anti breast cancer - acts on mts






11. Neuroglia






12. Phosphorylation - glycosloation - hyderoxylation






13. Substituting a purine for a pyrimdine or vice versa






14. RER translation of collagen alpha chains (preprocollagen) usually Gly-X-Y






15. One codon AUG






16. Enter G1 from G0 when stimulated Hepatocytes/lymphocytes






17. H1






18. HS1 - HSB - H2 - H4






19. Must be both activated and inactivated for cell cycle to progress






20. Attachment of ubiquitin to defective proteinds to tag them for breakdown






21. Splicing out of introns






22. Site of dteroid synthesis and detoxification of druigs and poisons (liver hepatocytes and steroid horomore adrenal cortex)






23. Inhibits bacterials dihydrofolate reducatese down thymine






24. Cleave terminal regions of procollagen to transform into insoluable tropocolagen






25. Tansport cellular cargo toward opposite ends of microtubule tracks






26. Epithelial cells






27. Change resulting in misreading of all nucleotides downstream - usually resulting in a truncated non functional protien






28. Proline - glycine






29. ATP- AMP (2 phosphoanhydride bonds)






30. AUG inAUGurates protein synthesis






31. DNA And RNA synthesized in the 5-3 direction






32. Connective tissue






33. Has enough energy to created the peptide bond






34. Vimentin - desmin - cytockeratin - glial fibrillary acid proteins - neurofilaments






35. 3 H bonds






36. Microtubule polymerization defect resulting in lowered phagocytosis. results in recurrent pyogenic infections - partial albinism and peripheral neuropathy






37. Type III






38. Inhibits by binding to the potassium side






39. Commonly results in dramatic decrease in amount of gene transcribed






40. Ribonucleotide reductase






41. RNA polymerase I makes rRNA - RNA pol II makes mRNA - RNA pol III makes tRNA






42. Intervening noncoding segments of DNA






43. Inhibits thymidylate synthase down thymine






44. Ketone






45. MRNA






46. Antigout - acts on mts






47. Prokaryotic only. Elongates leading strand by adding deoxynucleotides to the 3prime end. Elongates laggin strand. 3 prime to 5 prime exonuclease activity






48. Different exons can be combined to make nique protiens in different times






49. Unattached to any membrane; site of cytosolic and organeller prtoeins






50. Alpha 1 antitrypisn