* hat do you think holds together the various secondary structural elements in aParticular three-dimensional pattern? (Hint: Look back at Figure 4 - what issticking out from the sides of the a-helices and B-strands?)glutamic acidBCH,CHvalineCHH-NCHH.valinealanineCH2CH2lysineFigure 4-4 Essential Cell Biology 3/e (O Garland Science 2010)Figure 6. Three examples of bonding interactions that stabilize the tertiarystructures of proteins (indicated by arrows A, B,and C). Copyright 2013 from EssentialCell Biology, 4th Edition by Alberts et al. Reproduced by permission Garland Science/ Taylor &Francis LLC.CH2CH,SHSHCH2CH2OXIDATIONCH2SHREDUCTIONSHCH2CH2Figure 4-26 Essential Cell Bialogy 3e o Garland Science 2010)Figure 7. Disulfide bonds within proteins can form (left-pointing arrow) or bebroken (right- pointing arrow), depending on their chemical surroundings(oxidative or reducing). Copyright 2013 from Essential Cell Biology,4th Edition by Albertset al. Reproduced by permission of Garland Science/ Taylor & Francis LLC. Figure 7 shows one additional type of bond that can stabilize the tertiary structure of aprotein. This bond is called a disulfide bond (or disulfide bridge), and it involves thesulfhydryl (-SH) R groups from one particular type of amino acid. A disulfide bond canform only under certain conditions (oxidative conditions). We'll talk about oxidation andreduction next week. For now, just note that this type of bond does exist in someproteins.Answer the below questions on tertiary structure in your own document.8. Figure 6 shows examples of bonds that might stabilize the tertiary structure of aprotein (labeled A, B, and C). Do these interactions involve only the amino acid Rgroups, only the polypeptide backbone atoms, or both?9. In the table below, indicate what type of bond/ interaction is represented inthe examples shown in Figure 6, panels A, B, and C and whether eachinteraction involves group or backbone atoms.ExampleType of Bonding InteractionR group or backbone?BC10. For each of the three interactions shown in Figure 6, indicate how changes inthe following conditions might affect those interactions: pH, temperature, saltconcentration. Explain your answer.11. Which amino acid can form disulfide bonds? To help you answer, refer to aminoacid chart and Figure 7.12. What is different about the disulfide bond compared to the other types of bondsthat stabilize tertiary structure? Based on your existing knowledge of bonding, isthis bond weaker or stronger than the other types of bonds that stabilize tertiarystructure?13. Make a prediction of which tertiary interactions you might be more likely to find inthe proteins of prokaryotic species that live in the extreme environment of hotsprings compared to similar species that live in more moderate environments.Explain your answer.

These questions are about interactions in amino acids.

Answered: . Vwhat do you think holds together the…

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter16: Gene Expression

Section: Chapter Questions

Problem 3VCQ: Figure 16.13 An increase in phosphorylation levels of elF-2 has been observed in patients with...

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This is a homework question that I have on my Adv. Anatomy & Physiology assignment. How to I got about answering the question? (I do have the Codon table in my textbook) Consider a hypothetical protein that consists of the amino acid sequence arginine, phenylalanine and histidine. From this information, construct (1) the original DNA strand, (2) corresponding mRNA codons and (3) tRNA anticodons used to produce this hypothetical protein. (Only use 1 mRNA codon per amino acid.) In addition, be sure to include start and stop sequences where appropriate.
The CFTR membrane protein has an alpha helix that spans the membrane. The amino acid sequence of the central portion of this alpha helix, which is embedded within the membrane, is which one of the sequences below? Sequences are provided in the single letter code. a. VVVEVVVVEVVEEEVE b. VVVLVVVVLVVLLLVL c. VVVLVVVVREERRRER d. EEEREEEEREERRRER
Figure 16.13 An increase in phosphorylation levels of elF-2 has been observed in patients with neurodegenerative diseases such as Alzheimer’s, Parkinson's, and Huntington's. What impact do you think this might have on protein synthesis?
For transmembrane proteins, either single-pass or multi-pass, the membrane spanning part of the protein usually assumes which of the following motifs? βαβ αβα α-helix β-pleated sheet
Which amino acid sequence will form part of which protein structure, and why? Sequence 1: Ser-Phe-Gln-Val-Lys-Leu-His-Tyr-Asp-Val Sequence 2: Glu-Tyr-Leu-Asn-Phe-Ala-Gln-Val-Leu-Arg __Amphipathic beta strand __ Amphipathic alpha helix
Which of the following polypeptides would be most likely to form an a helix? Explain your answer. Cys-Arg-Ala-Gly-Asn-Arg-Lys-Glu-Thr-Tyr-Ile-Val-LeuSer-Glu-Asp-Asn-Phe-Gly-Ala-Pro-Lys-Ser-Ile-Leu-TrpGln-Lys-Ala-Ser-Val-Glu-Met-Ala-Val-Arg-Asn-Ser-Gly β sheets are less likely to form than a helices during the earliest stages of protein folding. Explainwhy this is the case. (hint: think about the hydrogen bonding requirements)
In what ways are spliceosomes and ribosomes similar? In what ways are they different? Can you suggest some possible reasons for their similarities?
If a quaternary (4°) protein structure has six N-terminus. How many total subunits does it have?
Polypeptides which are normally synthesized in the endoplasmic reticulum are about20 amino acids longer when they are synthesized by ribosomes not attached to the endoplasmicreticulum, What is the significance of this increase in length?
1a-The separation of the parent cell into two daughter cells fails to occur during the process of binary fission. Based on your knowledge of cell constriction in bacteria, what protein may be missing in the system (ie the protein was not expressed)? 1b-You are examining a novel protein and you notice that its final structure is at the secondary level. What type of bonds did you find that lead you to this conclusion? O a. Peptide bonds and hydrogen bonds O b. Covalent bonds and peptide bonds O c. Peptide bonds only O d. Hydrogen bonds only 1c- A peptide bond forms between. O a. The amino group of one amino acid and the carboxyl group of another amino acid. O b. The CH3 group of one amino acid and the carboxyl group of another amino acid. O c. The R groups of two amino acids. O d. A hydrogen of one amino acid and carbon of another amino acid.
An intermediate folding stage seen in protein denaturation or renaturation is called : a) domain b) motif c) subunit d) molten globule Proteins which do not renature spontaneously when denaturation conditions are removed may need the assistance of: a) a prosthetic group b) a higher salt concentration c) a lower temperature d) a chaperone protein The information needed for correct protein folding is encoded in: a) the surrounding molecules b) the protein’s amino acid sequence c) the pH of the aqueous medium d) the electrolyte composition of the aqueous solution
22-69 Indicate whether each of the following statementsrelating to protein synthesis is true or false.a. RNA is involved in both the transcription andtranslation phases of protein synthesis.b. DNA is the starting material for protein synthesis.c. The translation phase of protein synthesis convertsRNA to DNA.d. Transcription precedes translation in proteinsynthesis

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