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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. Contain the actual genetic information coding for protein






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






3. Read froma fixed starting point as a continous sequenecs of bases






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






5. Binds 50S blocking translocation






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






7. In the nucleus after transcitpion and only processed RNA is transporte out of the nucleus






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






9. Capping on 5 prime end (7 methylguanosine) -






10. Completed protein is released from ribosme through simple hydrolosis and dissociates






11. 1 RNA polymerase (multisubunite complex) makes all 3 kinds of RNA






12. Hn RNA






13. VItamin C






14. Anti breast cancer - acts on mts






15. Promoter - enhancer - promoter - TATA- transcription initiation site - coding region (including exons and introns) and then the AATAAA






16. Responsible for the accuracy of amino acid selection






17. Proline - glycine






18. Inhbits RNA pol II (found in death cap mushrooms)






19. Even 40S 60S =80S






20. Phosphorylation - glycosloation - hyderoxylation






21. Poly adenylation






22. Blocks denovo purine synthesis






23. You glyucosolate hte pro - alpha chain lysine resudens and form procollagen (triple helix of alpha chains)






24. A malfunction of mismatch repair (MUt L etc..)






25. Connective tissue






26. Changed aaconservative - new aa is similar in chemical structure






27. Close to - far from or even within (in an intron) the gene whose expression it regulates






28. Negatively charged DNA loops twice around histone octamers create a nucloesome bead.






29. More than 1 codon may code for the same amino acid






30. Xlinked recessive IV collagen bm - kidney - ear and eye -- nephritis and defness ocular disturbances






31. Prokaryotic only. Degrades RNA primer and fills in the gap with DNA (5 prime to 3 prime exonuclease)






32. Nucleotide excision repair - Base Excision repair - Mismath repair






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






34. CCA AT 3 PRIME END






35. Greater melting temperature lower fluidity






36. Lysine/hydroxylysine and combines to form collagen






37. Inhibits the atpase which increases intracellular sodium which increases intracellular calcium increases cardiaccontractility






38. Faulty collagen synthesis causing 1) hyperextensible skin 2) tendency to bleed 3) hypermobile joints






39. Inhibits 50S peptidyl transferase






40. Y shaped region along DNA template where leading and lagging strands are syntehsized






41. H1 string






42. (A - G) 2 rings Pure As Gold






43. Neurons






44. Substituting a pyramidine for a pyrimadine






45. Muscle






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






47. Anit helminth - act on microtubules






48. Each codon specifies only 1 amino acid






49. 3 H bonds






50. Tansport cellular cargo toward opposite ends of microtubule tracks