Name the two most common atoms hydrogen bonds within biological systems that give hydrogen a partial positive charge. 2. Are the atoms named in the question above in the backbone of the protein or are they found in R groups?  Which R groups? 3. Besides hydrogen, what other atom is involved in the hydrogen bonds in an alpha helix or beta sheet? In other words, hydrogen is interacting with what other atoms when it makes a hydrogen bond? 4. Write out, in order, the full names of the seven amino acids circled in the picture.

Q: 4. The interactions on the backbone (not the side chains) contribute to the (circle one):…

A: A protein is a polymer which is formed by a monomer amino acids that are linked together by peptide…

Q: 3. Amino acid residues and peptide bonds (a) Draw the chemical structure of F, S and H joined by…

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Q: 3. Supra-secondary structures of proteins - supercoiled alpha- helix, Greek key, meander, interlock,…

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Q: 3.Is the OH for the molecule in #2 from the carboxyl group or from the amino group? 4.Is the H for…

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Q: 5✓ The two central (a) Carbons: IX A Carbon atom in each side chain: The peptide bond is between…

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Q: List 4 tertiary interactions that exist in protein molecules and include what type of R groups (side…

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Q: 1. Which of the following structures could the following polypeptide form? And why? The non- polar…

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Q: 1. Please come up a peptide sequence for the two proteins shown in the diagram. Multi-pass protein…

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Q: 6. Peptide bonds link many amino acids into chains of subunits that make polypeptides, or proteins.…

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Q: 6. Discuss the potential contributions of ionic interaction, hydrogen bonds, hydrophobic…

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Q: 1. Name and draw the structures of standard amino acids that would likely form hydrogen bonds with…

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Q: Describe how each of the following relates to protein configuration: primary structure - secondary…

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Q: 5. In the early days of protein biochemistry, these proteins were described using "operational…

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Q: 1. Draw the tripeptide: Val-Leu-Met at pH 7 with the N-terminus to the left and C-terminus to the…

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Q: Which of the following is incorrect about the beta sheet? Parallel beta sheets are less stable than…

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Q: Please describe what is a peptide bond? What is the significance of the amino terminus versus the…

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Q: 9. Metabolically active tissues require lots of ATP, and making lots of ATP requires lots of oxygen.…

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Q: sheets are less likely to form than α helices during the earliest stages of protein folding. Explain…

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Q: 4. Which level of protein structure do proteins need to function (there may be more than one correct…

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Q: 5. The amino acid sequences of three peptide fragments are shown below. Peptide 1: QAMGRAGDLKYLGLHSV…

A: Hi! Thank you for the question. We are authorized to answer three subparts at a time, since you have…

Q: Explain 3 benefits of proteins forming higher oligomeric states.

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Q: 3. Compare the molecular property of amino acids and their roles in protein folding. (psa, logP,…

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Q: Which of the following statements about alpha-helix and beta-sheet structure are true? More than one…

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Q: 7. Why proteins prefer to have a-helices or ẞ-sheets in their interior core, instead of random coil…

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Q: Understand that some amino acids are nonpolar, polar/uncharged, charged. Explain how this is related…

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Q: 40. What would you expect about the formation of an alpha-helix for a segment of a protein chain…

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Q: 3. Proteins are important for numerous functions in a cell and their activity/function is dependent…

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Q: 9. The functions of proteins in the human body: the catalytic, structural, regulatory, contractile,…

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Q: 5. Indicate whether the following amino acid residues would be more likely to be found on the…

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Q: 7. What level of protein structure is retained when proteins unfold? Using what you know about the…

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Q: 9. Look at the protein below. Label the diagram on the right and show which part of the protein has…

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Q: c. Label each amino acid as polar, non-polar, or electrically charged d. Label the N-terminus and…

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Q: 17. Protein folding results in a large decrease in entropy since a polypeptide is now constrained…

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Q: 4. Cis peptide bonds are rarely found in proteins because they are about 8 kJ/mole less stable than…

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