A protein has a mutation of a glycine to a lysine. Which best predicts the impact of this mutation on the overall protein structure and function? H *NH, Glycine Lysine O A small hydrophobic amino acid has been replaced with a large hydrophilic amino acid, and this may change folding O A small hydrophilic amino acid has been replaced with a large hydrophobic amino acid, and this may change folding O These residues are similar in chemical properties, and there will be little impact on folding O This mutation may disrupt hydrogen bonds, which would disrupt the tertiary structure

A protein has a mutation of a glycine to a lysine. Which best predicts the impact of this mutation on the overall protein structure and function? H *NH, Glycine Lysine O A small hydrophobic amino acid has been replaced with a large hydrophilic amino acid, and this may change folding O A small hydrophilic amino acid has been replaced with a large hydrophobic amino acid, and this may change folding O These residues are similar in chemical properties, and there will be little impact on folding O This mutation may disrupt hydrogen bonds, which would disrupt the tertiary structure

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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Indicate which of the amino acid residues in the following peptide sequence contains a group that has a positive charge for its most likely charge state at pH 10. Asp-Tyr-Lys-GIn-Thr-Ile-Phe-Met-Ser (If none of the amino acids fit the criterion, select "none".) Asp Tyr ооооооооо Lys Gln Thr lle Phe Met Ser none
Part B Assume a protein is composed of 120 amino acid residues and that each amino acid can have three possible orientations. How many total possible orientations are there for the protein? Express the number of possible orientations to three significant figures. —| ΑΣΦ 1.797 • 1057 Each possible orientation of an amino acid is due to rotation about a bond. Since there are two terminal amino acids, there will be one fewer peptide bond compared to the number of amino acids. No credit lost. Try again. Submit ? Previous Answers Request Answer orientations
Which type of motifs/folds are found in the protein shown below Coiled-coil O EF Hand O Horseshoe O Rossmann O Jelly roll O Greek key O Alpha/beta barrel O Beta barrel O Beta sandwich OZinc finger
+H₂N-CH-COO™ 1 CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. O amino acid B amino acid D amino acid A amino acid E +H₂N-CH-COO™ 1 CH₂ T O amino acid C CH₂ 1 C=0 B. This amino acid participates in hydrophobic interactions to stabilize protein conformation. +H₂N-CH-COO™ I CH₂ I OH C. +H₂N-CH-COO™ I CH H₂C CH3 D.
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)
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?
3. Amino Acid Sequence and Protein Structure 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. 1 3 5 6 7 8 9 10 Ile - Ala - His - Thr - Tyr - Gly - Pro - Phe-Glu – Ala- - 11 12 13 14 15 17 20 Ala - Mat - Cys- Lys - Trp - Glu-Ala-Gln-Pro - Asp- 16 18 19 21 22 23 24 25 26 27 28 Gly - Met-Glu - Cys - Ala - Phe - His - Arg (a) Where might bends or ß turns occur? (b) Where might intrachain disulfide cross-linkages be formed? (c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, lle, Thr, Ala, Gln, Lys. Explain your reasoning.
Tertiary structures refer to the three-dimensional arrangement of every atom in the molecule. On the other hand, primary structures refer to the stable arrangements of amino acid residues in a protein that give rise to recurring patterns. O Both statements are correct O Both statements are incorrect O The first statement is incorrect while the second statement is correct O The first statement is correct while the second statement is incorrect
A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown below. Only one of the Cys has a free –SH group and the other two are involved in an -S-s- bond.
Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?
Which statement is true about protein folding? ○ The equilibrium between folded and unfolded states is best determined by measuring the time course of unfolding ○ Refolding of a protein typically exhibits a linear dependence on the concentration of denaturant ○ The sigmoidal shape of the unfolding transition reflects the complex architecture of proteins ○ Proteins with stable folding intermediates usually exhibit smooth free-energy funnels ○ The rate of unfolding increases as the temperature increases towards the Tm value
Make a comparison between the teasons for the different flexibility that proteins that consists mainly of a beta sheet structure compared to proteins that consist mainy of alpha helices.