Microbiology: An Evolving Science (Fourth Edition)
4th Edition
ISBN: 9780393615098
Author: John W. Foster, Joan L. Slonczewski
Publisher: W. W. Norton & Company
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Chapter 10.6, Problem 1TQ
Summary Introduction
To review:
The identification of phosphorylation and acetylation on proteins using tandem mass spectrometry (MS-MS).
Introduction:
The process of adding a phosphate group to an organic compound in a biochemical reaction is known as phosphorylation. It plays an important role in regulating many cellular processes like signal transduction pathways, cell cycle, and apoptosis. Acetylation is a process that involves the introduction of an acetyl
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Which of the choices are types of posttranslational modifications a newly synthesized protein may undergo? Select all the
choices that apply.
changes to hydrogen bonding capabilities
formation of an amide bond between Cys and an isoprenyl group
removal of prosthetic groups
removal of the thiol group from a Cys residue
modulation of charges on amino acids
proteolytic cleavage
covalent attachment of oligosaccharides to Asn, Thr, or Ser
When sequencing proteins, one tries to generate overlapping peptides by using cleavages at
specific sites. Which of the following statements about cleavages caused by particular chemicals or
enzymes are true?
Cyanogen bromide cleaves at the carboxyl side of threonine.
Chymotrypsin cleaves at the carboxyl side of aromatic amino acids.
Trypsin cleaves at the carboxyl side of Lys and Arg.
Chymotrypsin cleaves at the carboxyl side of aspartate and glutamate.
What is meant by denaturation of proteins? Give examples of protein denaturating agent?
Chapter 10 Solutions
Microbiology: An Evolving Science (Fourth Edition)
Ch. 10.1 - Prob. 1TQCh. 10.2 - Prob. 1TQCh. 10.2 - Prob. 2TQCh. 10.2 - Prob. 3TQCh. 10.2 - Prob. 4TQCh. 10.2 - Prob. 5TQCh. 10.3 - Prob. 1TQCh. 10.3 - Prob. 2TQCh. 10.4 - Prob. 1TQCh. 10.5 - Prob. 1TQ
Ch. 10.5 - Prob. 2TQCh. 10.6 - Prob. 1TQCh. 10 - Prob. 1RQCh. 10 - Prob. 2RQCh. 10 - Prob. 3RQCh. 10 - Prob. 4RQCh. 10 - Prob. 5RQCh. 10 - Prob. 6RQCh. 10 - Prob. 7RQCh. 10 - Prob. 8RQCh. 10 - Prob. 9RQCh. 10 - Prob. 10RQCh. 10 - Prob. 11RQCh. 10 - Prob. 12RQCh. 10 - Prob. 13RQCh. 10 - Prob. 14RQCh. 10 - Prob. 1TQCh. 10 - Prob. 2TQCh. 10 - Prob. 3TQCh. 10 - Prob. 4TQ
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- a) what does this suggest. b) suggest a macromolecule where this modification might occurarrow_forwardThe following proteins were separated by SDS-PAGE in the presence of mercaptoethanol. Sketch the relative positions of the various polypeptides on the gel. Label the positive and negative ends of the gel.Protein A: 40 kDa single polypeptideProtein B: 80 kDa protein, made up of two subunits of molecular weight 20 kDa and 60 kDa, held together by noncovalent interactionsProtein C: 200 kDa protein, made up of four identical subunits (50 kDa each) linked together by disulfide bondsarrow_forwardUse the given experimental data to deduce the sequence of an octapeptide that contains the amino acids Met, Ser (2 equiv), Ile (2 equiv), Gln, Val, and Ala. Edman degradation cleaves Ser from the octapeptide, and carboxypeptidase forms Val and a heptapeptide. Partial hydrolysis forms the following fragments: Ser, Met-Ile-Ala, Ala-Ile-Val, and Ser-Gln-Met-Ile. Be sure to answer all parts. (select) v-(select) -(select) v(select) ♥- (select) v (select) ♥ - (select) v-(select) varrow_forward
- Briefly describe the usage of Edman degradation to determine the primary structure of a protein.arrow_forwardDescribe the process used in purification of proteinarrow_forwardA protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol, three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein and clearly explain how you came to this determination.arrow_forward
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