There is a special initiator amino acid needed in prokaryotes, why is this the case? How does Eukaryotes go about handling this?
There is a special initiator amino acid needed in prokaryotes, why is this the case? How...
Polymerization of amino acids into a polypeptide requires energy. In terms of chemical thermodynamics, the chemical energy for peptide bond formation in translation technically comes from: hydrolysis of GTP hydrolysis of ATP translocation of the ribosome as it moves along the mRNA ribosomal RNA (rRNA) secondary structure transcription of the mRNA that is being translated Transfer RNA (tRNA) is a ribonucleic acid about 50-60 nucleotides long. When a tRNA gets "charged" by covalent addition of its cognate amino acid, to...
1. How does transcription and translation differ in Eukaryotes and in prokaryotes. 2. How is DNA transcription different from prokaryotes and Eukaryotes? 3. What is a gene?
6. Why is it necessary to wear latex gloves when handling the amino acid chromatogram? 7. An amino acid travels 2.5 cm from the origin on a paper chromatogram, and the solvent front travels 7.5 cm. Show the calculation for the Rf value of the amino acid? 8. Why should a pencil – not a pen --- be used to mark the origin on a paper chromatogram? 9. What precautions should be observed in this experiment?
How do prokaryotes and eukaryotes differ with respect to the number of open reading frames that are contained in a typical mRNA? Why does this difference make sense in view of the translation initiation strategies used by each type of organism? What consequences does this difference have for the regulation of coordinated gene expression in the two types of organisms—for example, how might a key regulator turn on a suite of related genes in prokaryotic or eukaryotic cells?
Does the amino acid proline contain a planar ring? If not why?
Lecture 3 Identify amino-/carboxy termini, and R-group on amino acid What is chirality? Identify a carbon that is chiral (i.e., has 4 different groups attached) Chiral compounds rotate plane polarized light Memorize amino acid 1) structure, 2) classification (hydrophobic, aliphatic, aromatic, negatively charged, positively charged, polar uncharged) Be able to draw glycine (the generic amino acid) Given an amino acid structure and pKas of ionizable groups, be able to determine the charge at pH 1, pH 14, and pH 7...
1. How and why could a protein change with a change in one amino acid? (Hint: think of Hemoglobin S)
3. Both glucose and amino acid claim to have a special relationship with their respective transport proteins. What is the basis for their claims?
For the following amino acids - explain why the overall charge on the amino acid is different at PH's 2, 7, and 11. Relate it to the pk, of the groups on the molecules To achieve distinction, you must explain that the form of an amino acid, whether positively charged, negatively charged or neutral, depends on the pH of the solution and also on the Ka of the acid group
Explain how/why the amino acid glycine and proline significantly impact the evolution of protein structure and function.