Which of the following amino acids can form 2 H-bonds within an alpha helix?Proline at position 6 in the sequenceGlycine at postion 2 in the sequenceProline at position 4 in the sequenceGlutamic acid at position 6 in the sequence

The question is all about the amino acid that are simplest form of protein by which a protein can be…

Answered: Which of the following amino acids can…

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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What forces contribute to the folding of a polypeptide? Can you explain the reasoning too?
A B 10 Refer to the following figure. How many H-bonds would be present in the four base pairs that are indicated in this sequence: C) 8 D) 12 TT T·* сссG | | | | & E die
Consider an alpha-helix comprised of twelve amino acid residues. How many hydrogen bonds should be formed between backbone atoms in this helix?
Within a naturally-occurring polypeptide, under neutral pH conditions (pH = 7.0), which of the following amino acids always has a negatively charged carboxyl group? the first amino acid in the primary structure histidine lysine arginine the last amino acid in the primary structure
The bottom peptide segment is found in the secondary structure composed of anti-parallel - sheets. From the C-terminus of the peptide below, the sequence immediately after alternation contains the following amino acid residues (from N → C) A-F-R-M-Y-A. a) which side do you expect to face the solvent? Briefly explain your reasons NH, но Nterminus
QUESTION 8 The Bohr effect refers to the decrease in affinity of Hb for 02 when the pH goes up. A. the decrease in affinity of Hb for 02 when the pH goes down. B. the increase in affinity of Hb for O2 when the 02 concentration goes up. C. the decrease in affinity of Hb for O2 when the BPG concentration goes up. OD. the decrease in affinity of Hb for O2 when the BPG concentration goes down. OUESTI ON 9
A 16-year-old female is recently diagnosed with a deficiency of muscle glycogen phosphorylase. She and her family are concerned and ask the following questions. Based on what you know about skeletal muscle glycogenolysis and muscle metabolism, please respond to each question with a thoughtful answer that describes the metabolism in these various scenarios in language that your patient will understand, while also being sure to include the role of the relevant metabolic pathways, specific enzymes, and stimulus for their activity: I’m not sure I understand the issue. Can you explain how muscle glycogen is used normally during exercise? I really like to take long walks; will Istill be able to do this with my friends? As a result of this deficiency, will I need to get up at night to eat to maintain my blood glucose levels? Do I need to worry about producing excessive lactate during intense anaerobic exercise?
Which of the following is/are least likely to be found in an alpha helix because it has an inappropriate Phi angle. a Polar charged amino acids b Proline c Nonpolar amino acids d Glycine e Polar uncharged amino acids
Which of the following best describes how the secondary structure of a protein is formed? A B с D O=U a-helix H O=C N-H R-C-H C=0 H-N H-C-R O=C N-H R-C-H C=O H-N O-C N-H R-C-H C=O H-N N-H 0= H-C-R H-N C=O R-C-4 N-H O=C H-C-R 4-1 Ç=O R-C-H N-H 0=C H-C-R (=O R-C-H B-pleated sheet ionic bonds between the R groups of the polypeptide amino acids -Uh hydrogen bonds between the carboxyl and amino groups of non-adjacent amino acids covalent bonds between the carboxyl and amino groups of adjacent amino acids hydrogen bonds between the R groups of the polypeptide amino acids

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