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

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.)
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? [
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
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.
b) It's said that secondary structures form because of intra- and intermolecular hydrogen bonding involving the peptide bond. Describe what is going on to further stabilize secondary structure through these interactions.
The amino acid arginine ionizes according to the following scheme: (a) Calculate the isoelectric point of arginine. You can neglect contributions from form I. Why? (b) Calculate the average charge on arginine when pH = 9.20. (c) Is the value of average charge you calculated in part b reasonable, given the pI you calculated in part a? Explain your answer
Glutamine is an amino acid that has -CH₂-CH2-CO-NH₂ as its R group. The R group of the amino acid isoleucine is -CH2-CH-(CH3)2. If these amino acids were in a globular protein in aqueous solution, where would they most likely be? O Both glutamine and isoleucine would be in the interior and on the exterior of the globular protein. O Glutamine would be in the interior, and isoleucine would be on the exterior of the globular protein. O There isn't enough information O Both glutamine and isoleucine would be on the exterior of the globular protein. O Isoleucine would be in the interior, and glutamine would be on the exterior of the globular protein.
Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.
Provide the correct three-letter abbreviation for the following amino acid: O || H₂N-CH-C-OH I CH₂ CH₂ C=O I NH₂
Determine the sequence of the following 10-mer of ferritin using the data below. i. Complete acid hydrolysis of the 10-mer results in identification of 1A, 1D, 1E, 1F, 1H, 1K, 2L, 1T, 1Y ii. Digestion of the 10-mer with chymotrypsin results in 3 fragments containing (D, H, K, T), (F, L) and (A, E, L, Y) iii. Digestion of the 10-mer with V8 protease, which cuts on the C-side of acidic amino acids, results in three fragments containing (D, F, L, Y), (A, E, L) and (H, K, T) iv. Digestion with trypsin results in a fragment H-T and a fragment with all the other amino acids v. Treatment of the 10-mer with FDNB followed by complete acid hydrolysis results in the following two derivatives, DNP-1 and DNP-2 vi. Treatment of the 10-mer with a carboxypeptidase results in a free threonine

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