X What is a characteristic of both an alpha-helix and a beta-pleated sheet? * 0/1 Both can be anti-parallel structures Both form interactions involving the oxygens of peptide bonds Both are found only within multimeric proteins Both are denatured when heat breaks peptide bonds Correct answer Both form interactions involving the oxygens of peptide bonds ×

X What is a characteristic of both an alpha-helix and a beta-pleated sheet? * 0/1 Both can be anti-parallel structures Both form interactions involving the oxygens of peptide bonds Both are found only within multimeric proteins Both are denatured when heat breaks peptide bonds Correct answer Both form interactions involving the oxygens of peptide bonds ×

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter3: Biological Molecules: The Carbon Compounds Of Life

Section: Chapter Questions

Problem 8TYK: The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices...

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LLNSAMSRLYSLRSS 1.Assuming this sequnce is enitrely alpha helical what is the hydrogen bond donor to the carbonyl oxygen of Met6? 2.what amino acids in the sequnce above would most likely face the hydrophoic core od a protein? 3. at ph7 which amino acid side chain can form ionic bonds.
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Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data Consider the following amino acid sequence Ile-Ala-His-Thr-Tyr-Gly-Pro-Phe-Glu-Ala-Ala-Met-Cys-Lys-Trp-Glu-Ala-Gln-Pro-Asp-Gly-Met-Glu-Cys-Ala-Phe-His-Arg Where might reverse turns occur? Where might Intrachain disulfide linkages be formed? What will be the secondary structure formed from this sequence? Assuming that this sequence is part of a larger globular protein, indicate the probable location of the following amino acid residues: Asp, Ile, Thr, Ala. Gln, Lys.( Hint: see Hydropathy index)
The amino acid sequence of three peptide fragments are shown below. Peptide 1: QAMGRAGDLKYLGLHSV Peptide 2: ALMALFMVMALVLVSVLFIA Peptide 3: MVEDLLKQIARYLISE (a) Circle all of the charged residues in peptide 1 (assume pH =7.0). Box all of the aromatic residues in peptide 2. Underline all of the nonpolar residues in peptide 3. (b) Determine the net charge of the predominant form of each of the peptides at pH 4.5 and pH 11.5. Assume the ionizable groups have the pKa values listen in Table 2.1 of your text. (c) Which of these peptides would be most likely to be found as an alpha helix in a soluble (cytoplasmic) protein? Which would be most likely to be found as an alpha helix in a transmembrane protein? Which would be least likely to form an alpha helix of any kind?
What maintains the secondary structure of protein: A) peptide bond. B) Hydrogen bonds between the amino group of one peptide bond and the carboxyl group of another peptide bond. C) Hydrogen bonds between the R group of one amino acid and the carboxyl group og another peptide bond. D) disulfide bonds. E) Hydrophobic interactions.