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Indicate whether the following peptides are hydrophilicor hydrophobic:
- a. MLWILAA — hydrophobic
- b. VAIKVLIL — hydrophobic
- c. CSKEGCPN — hydrophilic
- d. SSIQKNET — hydrophilic
- e. YAQKFQGRT — hydrophilic
- f. AAPLIWWA — hydrophobic
- g. SLKSSTGGQ — hydrophilic
Is the following peptide positively or negativelycharged at neutral pH?
Answer: The peptide is positively charged.
The peptide is positively charged.
Consider an RNA template made from a 2:1 mixture of C:A.
What would be the three amino acids most frequently incorporated into protein?
would be most frequently incorporated.
What is the peptide sequence encoded inAUAUAUAUAUAUAUA . . .?
The peptide sequence would alternate isoleucine (AUA) and tyrosine (UAU):
IYIYI. . . .
Write the anticodons 5' to 3' of the following aminoacids:
- a. L — UAA, CAA, AAG, GAG, UAG, CAG
- b. T — AGU, GGU, UGU, CGU
- c. M — CAU
- d. H — AUG, GUG
- e. R — ACG, GCG, UCG, CCG
- f. I — AAU, GAU
A protein contains the sequence
What is the likely function of this protein?
(Note: See Box A3-4 p57.)
This protein has a leucine residue at sequential 7th positions forming a leucine zipper,found in transcription factors. The conserved sequence has leucine or other hydrophilic residue at each 7th position so that the leucine side chains radiate outward to facilitate associations with other peptides of similar structure.
A histone-like protein contains the sequence:
What characteristic of this sequence makes it likely to associate with DNA?
This protein is positively charged, which would facilitate association with negatively charged DNA.
A procedure for digestion of DNA with a restrictionenzyme includes a final incubation step of 5 minutesat 95ºC.
What is the likely purpose of this final step?
The 95ºC incubation will inactivate theprotein, preventing its activity in subsequentsteps of the assay.
What is a ribozyme?
A ribozyme is an RNA molecule that canmetabolize other molecules like an enzyme.
Name the nonprotein prosthetic groups for the following conjugated proteins:
- glycoprotein — sugars
- lipoprotein — lipids
- metalloprotein — metal atoms