An amino acid is connected to the t-RNA by which of the following functional groups? a. Ester b. Amide c. Carbamate d. Ether
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- A heptapeptide was analyzed by Pinky. She reacted it with carboxypeptidase and found out that it reacted with proline. Partial hydrolysis of the heptapeptide gave the following shorter peptides: Tyr-Leu Ser-Arg Tyr-Trp-Ser Tyr-Leu-Pro What is the sequence of the heptapeptide? Input the three-letter codes of the amino acids separated by dashes with no space character (e.g. Arg-Ser-Leu).Which of the following does cytosine pair with? a. guanine b. thymine c. adenine d. a pyrimidineIdentify which of the following pairs of amino acid residues can have hydrogen bonding between their side chains. A. Alaine and Glycine B. Leucine and Isoleucine C. Valinc and Asparaginc D. Threonine and Tryrosine
- Compare and contrast the biological roles of the following amino acids the following pairs ofamino acids. Once you have documented these role state which member of the pair is most important and why.Select the amino acids that are most likely to participate in hydrophobic interations. SELECT ALL THAT APPLY A. Valine B. Leuicine C. Phenylalanine D. AspartateDetermine the synthetic family to which each of the following amino acids belongs:a. alanineb. phenylalaninec. methionined. tryptophane. histidinef. serine
- Which of the following pairs of amino acids can have intermolecular hydrogen bonding between the functional groups in their side chains? Select all that apply. phenylalanine and tyrosine two tyrosine residues serine and threonine alanine and threonineName an example of each of the following classes ofcompounds:a. glycoproteinb. proteoglycanc. disaccharided. glycosaminoglycan (GAG)Show anabolism of two molecules of serine. Be sure to clearly identify each molecule and bond/linkage involved. Hand-draw the diagram
- Umoles SH 2. ASE-3: A polypeptide that has the smell of a rotten egg was extracted from plant. You being a good MD with excellent knowledge of biochemistry performed the following: Titrated the polypeptide with DTNB. The absorbance of the obtained yellow color was 0.16. I. 1. Compared to a standard curve of-SH (Curve A below ), the estimated free -SH is A. Not possible to determine unless the polypeptide amino acid composition is known B. 1 umole of Cys C. 1 umole of either methionine or cysteine 2. Treatment of the polypeptide with DTT followed by DTNB yielded an absorbance of 0.81, indicating that the polypeptide: A. Contains 5 disulfide bridges B. Contains 5 Cys C. Was inaccurately titrated in the above situation yielding lumole D. Contains 3 intra-molecular disulfide bridges. 5. 4. 1. 0.2 0.4 0.8 1. Abs orbance 3. The polypeptide is composed of deca and nona peptides with: N- terminals of ala and val respectively and C-terminals of asn and lys respectively. The Decapeptide is…A pyrimidine(s) with a H-bond acceptor its middle position is/are a Cytosine b Uracil c Cytidine d ThymineA protein is allosterically regulated by a molecule. This molecule enhances the binding affinity, and is different from the normal ligand. How would you describe this molecule? A negative homotropic molecule A negative heterotropic molecule A positive heterotropic molecule A positive homotropic molecule