A variety of organic chelating ligands have been synthesized totightly coordinate radioactive metal cations to identify and treat malig-nancies by coupling the metal complex to a polypeptide linker attachedto a monoclonal antibody that binds specifically to a cell surface re-ceptor. One such metal complex is illustrated in the diagram on theright. The radioactive Cu-64 cation is tightly coordinated by the che-lating ligand that is, in turn, conjugated to a peptide linker attached toa monoclonal antibody. (The antibody is not shown in this diagram.)When coupled to a specifically designed monoclonal antibody, thecomplex binds specifically to somatostatin receptors that are ex-pressed on the surface of neuroendocrine tumors. Subsequently theentire complex with the receptor is internalized, i.e., passed into thecytoplasm, where the radioactive metal cation kills the malignant cell.1.CH3HN NHNHHN NHNHHNНоНОNHHNS-SHNНоNHNHHN-NH HN-H2NOHNH) Write the three letter abbreviations and sequence numbers of the amino acid residues joined(d) (through the disulfide bridge. If this bridge were found for the two joined amino acids free in solution,what is the special name given to this molecule? Are the sulfur atoms in the disulfide bridge in anoxidized or a reduced state?

Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

Answered: (d) ( through the disulfide bridge. If…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

The structures of three amino acids are given as below. Glycine -H Cysteine - CH2 - SH Glutamate - CH2 CH2 (i) Describe the properties of each of these amino acids. (ii) Draw the tripeptide Glu-Cys-Gly.
Consider a protein in which a negatively charged glutamic acid side chain (pKa=4.2) makes a salt bridge (ion-ion interaction) with a positively charged histidine side chain (pKa=6.5). Part C: Justify your answer with calculations of partial charges on these amino acid side chains at pH=7.9.(Hint: Consider lessons from Coulomb's law, and the Henderson-Hasselbalch equation.)
Describe the chemistry involved in the processes of Lipid Interesterification and Lipid Fractionation. How can these two processes be combined to provide a spreadable lipid from palm oil? (Please provide a detailed explanation).
B) An aqueous solution (pH ~7) containing mixture of three amino acids; glycine (G), arginine (R) and glutamic acid (E), was dropped onto center of a solid matrix (e.g chromatographic paper) which is incorporated in an electrical circuit (a). After applying electrostatic potential, the aminoacids are separated as shown in b. Determine amino acids that are labeled as 1, 2 and 3. a) DC Power Supply (OFF) b) DC Power Supply (ON) Solid matrix Solid matrix Cathode Anode Cathode Anode buffer buffer buffer buffer Sample containing amino acids G, R, E
A) Refer to the figure below, Identify and explain the two types of reactions, and describe what are the importance of these reactions to our bodies. Reaction 1 H Monomer Reaction 2 H H OH + H H H₂O H H₂O OH + H H OH OH + H H₂O H₂O OH OH + H OH OH OH OH B) What are the main chemical interactions that determine and maintain the quaternary structure of proteins. Also, what are the conditions that can alter these interactions? [
Will the following amino acid migrate in an electric field? Explain.
In case of the same amino acid as in the picture, in which ionization state would this amino acid be at (i) a pH that will correspond with the pI-value and (ii) a pH below the pI-value?
This amino acid is: (Note that the non-ionized form is shown; remember that backbone groups are irrelevant to classification) a) Polarized (+) charged b) Nonpolar c) Polar and (-) charged d) Polar uncharged
What is the contribution of dilsulfide bonds in proteins?Which groups or side chain participate in these reactions? Discuss with examples in detail.
a. what general category would you place this molecule in of the four categories of biomolecules? b. List 5 functional groups you see in this molecule?
A tetrameric protein dissociates into dimers when the detergent sodium dodecyl sulfate (SDS) is added to a solution of the protein. But the dimers are termed SDS-resistant because they do not further dissociate into monomers in the presence of the detergent. What intermolecular forces might be acting at the dimer-dimer interface? Are the intermolecular forces acting at the monomer-monomer interface different? Explain.
Among these amino acid combinations listed above, only the combination of Lys and Glu have side chains with groups that have the greatest ability to stabilize the tertiary structure of a protein. Explain by drawing (a) why Lys and Glu side chain interaction stabilizes the tertiary structure of a protein (b) why the pairs of Glu and Asp & Arg and Pro cannot provide the stability to the protein structure.

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