Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Chapter 2, Problem 22P
Interpretation Introduction
Interpretation:
The reason for glycine to be highly conserved as an amino acid residue in the protein’s evolution needs to be explained.
Concept introduction:
Amino acids are organic compounds containing amino as well as
Here, R group is different for different amino acids. This group can be acidic, basic or neutral.
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Peptide mass determination. You have isolated a proteinfrom the bacterium E. coli and seek to confirm its identityby trypsin digestion and mass spectrometry. Determinationof the masses of several peptide fragments has enabled youto deduce the identity of the protein. However, there is adiscrepancy with one of the peptide fragments, whichyou believe should have the sequence MLNSFK and an(M 1 H)1 value of 739.38. In your experiments, yourepeat edly obtain an (M 1 H)1 value of 767.38. What isthe cause of this discrepancy and what does it tell youabout the region of the protein from which this peptide isderived?
Chapter 2 Solutions
Biochemistry
Ch. 2 - Prob. 1PCh. 2 - Prob. 2PCh. 2 - Prob. 3PCh. 2 - Prob. 4PCh. 2 - Prob. 5PCh. 2 - Prob. 6PCh. 2 - Prob. 7PCh. 2 - Prob. 8PCh. 2 - Prob. 9PCh. 2 - Prob. 10P
Ch. 2 - Prob. 11PCh. 2 - Prob. 12PCh. 2 - Prob. 13PCh. 2 - Prob. 14PCh. 2 - Prob. 15PCh. 2 - Prob. 16PCh. 2 - Prob. 17PCh. 2 - Prob. 18PCh. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21PCh. 2 - Prob. 22PCh. 2 - Prob. 23PCh. 2 - Prob. 24PCh. 2 - Prob. 25PCh. 2 - Prob. 26PCh. 2 - Prob. 27PCh. 2 - Prob. 28PCh. 2 - Prob. 29PCh. 2 - Prob. 30PCh. 2 - Prob. 31PCh. 2 - Prob. 32PCh. 2 - Prob. 33PCh. 2 - Prob. 34PCh. 2 - Prob. 35PCh. 2 - Prob. 36PCh. 2 - Prob. 37P
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- Alpha-helix of proteins, its characteristics. Draw a diagram of the arrangement of amino acids in the alpha helix. Examples of proteins formed mainly by this structure.arrow_forwardLong explanations are not needed. Answers and brief descriptions would be enough. During the formation of the peptide bond which of the following takes place? a. Hydrogen atom is lost from its carboxyl group of one amino acid and a hydrogen atom is lost from the amino group of another amino acid. b. Hydrogen atom is lost from its carboxyl group of one amino acid and a hydroxyl group is lost from the amino group of another amino acid. c. Hydroxyl group is lost from its carboxyl group of one amino acid and a hydroxyl group is lost from the amino group of another amino acid. d. Hydroxyl group is lost from its carboxyl group of one amino acid and a hydrogen atom is lost from the amino group of another amino acid.arrow_forwardShape and dimension. (a) Tropomyosin, a 70-kDa muscle protein, is a two-stranded α-helical coiled coil. Estimate the length of the molecule. (b) Suppose that a 40-residue segment of a protein folds into a two-stranded antiparallel β structure with a 4-residue hairpin turn. What is the longest dimension of this motif?arrow_forward
- Optical isomerism of amino acids. L and D amino acids. Chiral centers of amino acids. Give examples of amino acids that do not have optical isomers.arrow_forwardThe number of distinct protein folds in limited. Why might this be so?arrow_forwardIonization State of Histidine.Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation. 1.Histidine has three ionizable functional groups. Write the equilibrium equations for its three ion-izationsand assign the proper pKa for each ionization. Draw the structure of histidine in each ionization state.What is the net charge on the histidine molecule in each ionization state? 2.Which structure drawn in (1) corresponds to theionization state of histidine at pH 1, 4, 8, and12?Note that the ionization state can be approximated by treating each ionizable group independently. 3.What is the net charge of histidine at pH 1, 4, 8, and 12? For each pH, will histidine migrate to-ward the anode (+) or cathode (-) when placed in an electric field?arrow_forward
- Vertebrate proteins? What is meant by the term polypeptide backbone?arrow_forward. A nervous polecat. Pyrrolysine (Pyl, O) and Selenocysteine (Sec, U) are two uncommon amino acids. Knowing that these amino acids exists, translate the following amino acid sequence into one – letter code: Thr – Trp – Ile – Thr – Cys – His – Tyr – Leu – Ile – Thr – Thr – Ile – Glu – Phe – Glu – Arg – Arg – Glu – Thr – Ala – Arg – Glu – Asn – Thr – Tyr – Pyl – Sec – Met – Ala – Leu – Phe – Pyl – Tyr.arrow_forwardDraw any pentapeptide. All C-O, C-N, and C-S bonds must be written out, as well as all N-H, S-H, and O-H atoms/bonds. Your peptide must include at least one amino acid from each of the major classes of amino acids (i.e. charged, polar, etc.). Circle each peptide bond in this peptide.arrow_forward
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