4. In the following diagram of a portion of a protein, label the types of interactions that areshown.CHH;Ć `CH, |H;C _CH3 !CH- Polypeptidebackbonec=OHCH2-CH5–S}-CH,---CH;-CH-CH;-CH, NH," 0-C-CH,d.What level of protein structure are these interactions producing?

The structural organization of protein was classified into four different types and they are primary…

Answered: CH HC CH, | - Polypeptide backbone CH2…

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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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
Hydrophobic intercation associated with protein tertiary structure involve
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
What is the net electric charge of a peptide that has the sequence and provide the one letter code if you can Glu-His-Ser-Gly-Leu-Arg-Pro-Gly at pH 3, and 11
I-D-E-L-Y-S-Q-V-C-S-H-L-D-T-V-R This amino acid sequence forms an alpha helix. When thinking about how the helix folds into its tertiary strucutre, use entropy and enthalpy to explain what would happen energetically.
name and identify
9
I-D-E-L-Y-S-Q-V-C-S-H-L-D-T-V-R Circle the hydrophobic residues in the amino acid sequence above and box the hydrophobic residues.
A new amino acid is found with the alpha N and backbone COOH pKa's the same as histidine but with a neutral side chain. What is the isoelectric point of this new amino acid?
> Is the R group (CH3) on the amino acid alanine seen below, polar or non-polar? > If there were several alanines close together in a peptide chain would that bit of the chain be exposed to or folded to "hide" from water? H H N-C H-C-H 0-H
Peptide 1: QAMGRAGDLKYLGLHSV Peptide 2: ALMALFMVMALVLVSVLFIA Peptide 3: MVEDLLKQIARYLISE Which of these peptides would be most likely to be found as an a helix in a soluble (cytoplasmic) protein? Which would be most likely to be found as an a helix in a transmembrane protein? Which would be least likely to form an a helix of any kind? Briefly explain your answers.
In the tertiary structure of a protein, which pair of amino acid side chains would be most likely to participate in hydrogen bonds? Asn / Ala Ser / Cys Thr/Val Tyr/ Phe Gln/Thr

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CH HC CH, | - Polypeptide backbone CH2 HC CH, CH - CH2¬S–5}-CH,-- OH -CH;-CH;-CHy-CH, NH," 0-ċ-CH,- d. evel of protein structure are these interactions producing?