4. Do the "Bond X" bonds in Figure 4 involve atoms in the amino acid R groups or inthe polypeptide "backbone"/ “main chain" atoms?5. Given Your Answer To "b," are each of the following statements True or False?Be able to explain your reasoning.o Only very specific primary sequences can form a-helices and B-sheets.o Many different primary sequences can form a-helices and B-sheets.Each arrow depicted in Figure 4D represents consecutive amino acids in the primarysequence of the polypeptide, while the different arrows may be formed from aminoacids that are removed from each other in the primary sequence. Each arrow isreferred to as a B-strand, and the structure formed through interaction of the B-strandsis the B-sheet. In a complete protein, other segments of the protein would connect thedifferent B-strands.6. Do the "Bond X" bonds in the B-sheet connect atoms from the same B-strand orneighboring strands? amino acids are joined together bybónds, which are a particularbond.type ofSECONDARY STRUCTUREB sheeta helixamino acidside chainamino acidside chainBond Xhydrogencarbon.oxygennitrogenBond Xcarboncarbon-hydrogenpeptidebond„nitrogen-nitrogenoxygencarbonBFigure 4-10 Essential Cell Biology 3/e (© Garland Science 2010)Figure 4. Two types of secondary structure proteins: a-helix and B-sheet (constructedfrom multiple B-strands). A & B: a-helix structure represented in (A) ball-and-stick and(B) ribbon forms. C & D: B-sheet structure represented similarly. Copyright 2013 fromEssential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission Garland Science/Taylor &Francis LLC.Answer the below questions on secondary structure in your own document.3. The hatched lines connecting atoms in Figure 4 represent the bonds that holdtogether these secondary structures (for example, the bond labeled "Bond X").What types of bonds are these? (If you're having trouble seeing, these bondsare between an oxygen and a hydrogen atom, and a hatched line representsthe same type of bond as the dotted lines you encountered when discussingwater and the macromolecules.)

Answer is THE HATCHED LINE INDICATED THE HYDROGEN BONDS BETWEEN THE C=O. The polypeptide secondary…

amino acids are joined together by bónds, which are a particular bond. type of SECONDARY STRUCTURE B sheet a helix amino acid side chain amino acid Bond X hydrogen- ,side chain carbon. охудen nitrogen carbon Bond X carbon hydrogen peptide bond nitrogen nitrogen oxygen carbon A B Figure 4-10 Essential Cell Biology 3/e (O Garland Science 2010) C D Figure 4. Two types of secondary structure proteins: a-helix and B-sheet (constructed from multiple B-strands). A & B: a-helix structure represented in (A) ball-and-stick and (B) ribbon forms. C & D: B-sheet structure represented similarly. Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission Garland Science/Taylor & Francis LLC. Answer the below questions on secondary structure in your own document. 3. The hatched lines connecting atoms in Figure 4 represent the bonds that hold together these secondary structures (for example, the bond labeled "Bond X").

amino acids are joined together by bónds, which are a particular bond. type of SECONDARY STRUCTURE B sheet a helix amino acid side chain amino acid Bond X hydrogen- ,side chain carbon. охудen nitrogen carbon Bond X carbon hydrogen peptide bond nitrogen nitrogen oxygen carbon A B Figure 4-10 Essential Cell Biology 3/e (O Garland Science 2010) C D Figure 4. Two types of secondary structure proteins: a-helix and B-sheet (constructed from multiple B-strands). A & B: a-helix structure represented in (A) ball-and-stick and (B) ribbon forms. C & D: B-sheet structure represented similarly. Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission Garland Science/Taylor & Francis LLC. Answer the below questions on secondary structure in your own document. 3. The hatched lines connecting atoms in Figure 4 represent the bonds that hold together these secondary structures (for example, the bond labeled "Bond X").

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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On 4. Below is a polypeptide with an unknown number of amino acids. On the diagram below: a. Circle EVERY peptide bond b. Circle and number each amino acid from 1, 2, 3, and so on; from left to right c. Label each amino acid as polar, non-polar, or electrically charged d. Label the N-terminus and C-terminus e. Select three pairs of amino acids that could potentially interact to influence tertiary structure AND state the bond/force/interaction type involved in each pair. H₂N-CH-C-N-CH-C- CH₂ CH₂ CH₂ NH CINH NH₂ Accessibility: Investigate CH₂ -NH -CH-C-N- CH-OH CH3 -CH-C-N CH₂ CH₂ -N- OH CHIC-OH CH₂ OH
Match the protein structure terms on the left with the descriptions on the right. v (Choose ) commonly observed combinations of secondary structural elements tertiary structure Long segments of secondary structure. supersecondary structure basic component of quaternary structure Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the peptide Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the side chain compact structural or functional regions within a given polypeptide functional structures formed by non-covalent interactions between multiple polypeptides. domain (Choosel subunit quaternary structure (Choose)
Draw beta sheet with backbone hydrogen bonds, is this structure on the interior or exterior of the protein and why? Region 1: -Ser-Thr-Glu-His- Region 2: -Asp-Tyr-Lys-Asn
A change in the DNA that codes for a protein will cause a change in the [select all that apply] secondary structure tertiary structure primary structure protein function quaternary structure
8) The figure shows an unfolded polypeptide consisting of six amino acids. Describe how cooperativity will drive protein folding of the polypeptide chain into an alpha-helixe- 10EEHOW is AG changed as each amino acid is incorporated into the secondary structure - s)? O H O H 3 H. H. 5 CH-C H. 6 -N-CH-C- OH O H,N CH-C -N CH C-N CH CH CH2 CH2 CH2 CH2 CH OH CH H;C CH3
Choose the best statement regarding the R groups of amino acids in an alpha helix. Group of answer choices They are located in the interior of the helix. They stick out from the axis of the helix. They participate in H-bonds that stabilizes the helix. They are completely incompatible with helix formation.
The primary structure of a protein is shown below. Please answer the following questions. Leu-Arg-Ser-lle-Glu-Thr-Val-Val-Asn-Gln-Val-lle-Ser- Tyr a. Where is this section of the polypeptide most likely located [ Select ] completely embedded inside the protein partially exposed to the aqueous environment b. Is the above more likely an alpha helix or a beta-pleated sh completely exposed to the aqueous environment c. Which two amino acid residues are least likely to be in an alpha helix, but most likely to be a part of a beta turn? (Please select the amino acids in alphabetical order). [ Select ] [ Select ]
Draw two different AMINO ACID side chains forming H bond interactions with atoms on the major groove of the structure below. major groove N-Ho.. CH3 .•H-N Adenine R Thymine
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
In class we learned about the H-bonding pattern in an alpha-helix. Asp 61 of the spidroin CTD has a slightly unusual H-bonding feature within the helix. That is because it forms three H-bonds. They are H-bonds between its carbonyl oxygen and , between its amide hydrogen and , and between its side chain and Hint: by clicking once on the ribbon diagram at any spot, the model will show H-bonding in that spot.
1. what do you think a “peptide”means? 2. Proteins are extremely long, folded chains of amino acids, containing between 150-1000 amino acids linked together in a straight chain. A protein will have a long repeating chain of-N-C-C- as its backbone, with different R groups sticking out. How long could a protein be? be specific. 3. Add the C’s and H’s into their structural formulas. picture included
The human anti-bacterial protein lysozyme, consisting of a single polypeptide with 129 amino acids, contains how many peptide bonds? 131 peptide bonds 130 peptide bonds 129 peptide bonds 128 peptide bonds 127 peptide bonds