In the peptide shown below, a covalent bond that could rotate to form secondary structureis correctly identified / labeled by letter:ABOHstill fotDOBOCOOOBDFCOAHNENHOH"NH₂- F

There are two types of secondary structures are which are found in protein: alpha helix and beta…

Answered: In the peptide shown below, a covalent…

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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Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU
Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU I NEED IT ASAP PLEASE
Suppose that the given peptide below is a segment in a globular protein's primary structure. Determine what would most likely be the type of secondary structure that it will form. Explain. T-L-S-A-R-I-D-V
Draw peptide Pro-Ser-Ala-Phe-Glu as you would see it at pH 7. Include stereochemistry.
For the protein given in the attached picture: Write the name of these 5 amino acids corresponding to their abbreviation of 3 letters. Describe precisely how the functional groups in the amino acids are involved in bonding between two successive amino acids in the protein.
Given the following peptide, answer following questions 1-5: CO CH2 O || CH2 O H3N-CH-C-NH- CH-c-OCH3 | 1. Is this a dipeptide or tripeptide? 2. How many amino acid components/residues are there? 3. Name these amino acids. 4. What kind of bond links these amino acids? 5. The above structure represents the major ingredient in some commercial product(s). Identify the name of this major ingredient or the commercial product(s). Given that the hemagglutininin protein in influenza virus contains a remarkably long a-helix with 53 residues, answer questions 6-7. 6. How long is this a-helix (in nm)? Show all calculations. 7. How many turns does this helix have? Show all calculations.
Write the peptides of the full name " RYJO NNALAMBA" Every symbol of the Fullname writes the expanded structure in a zwitterion form. Then give the name of the polypeptide as a single molecule of the full name
A peptide has the sequence Glu-His–Trp–Ser-Gly–Leu-Arg-Pro–Gly The pK, values for the peptide's side chains, terminal amino groups, and carboxyl groups are provided in the table. Amino acid Amino pKa Carboxyl pKa Side-chain pKa glutamate 9.60 2.34 4.25 histidine 9.17 1.82 6.00 tryptophan 9.39 2.38 serine 9.15 2.21 glycine 9.60 2.34 leucine 9.60 2.36 arginine 9.04 2.17 12.48 proline 10.96 1.99 Calculate the net charge of the molecule at pH 3. net charge at pH 3:
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.
Draw the Ala-Ser-Leu-Asp polypeptide (perspective formula) showing the fully extended backbone geometry (all angles +/- 180°). Include correct stereochemistry for L-amino acids. Label all bond rotations representing the angles at each residue
Peptide A: V-E-S-A-L-D-I-F-R-T-A-L-S Peptide B: S-E-P-P-T-E-G-P Peptide C: T-L-S-A-R-I-D-V Suppose that peptides A, B and C are peptides in a globular protein. Give a possible structural motif or supersecondary structure that can be formed by repeating units of the given three peptides.
T/F: The titration curve for serine will have 2 inflection points. T/F: The Amino Acid D-selenocysteine has an R-Configuration T/F: Each water molecule can form H bonds with 4 other water molecules T/F: In a buffer system, decreasing the concentration of the conjugate base relative to acid makes the buffer more acidic T/F: Glycine forms good interactions in a protein structure True or false?

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In the peptide shown below, a covalent bond that could rotate to form secondary structure is correctly identified/labeled by letter: B E OH Thil fond OE OC B D C OF OA D HN NH OH "NH₂ F