8. Explain the role of post-translational modifications of protein molecules: the formation of disulfide bridges, hydrolysis of peptide bonds under the action of specific proteases, glycosylation, phosphorylation / dephosphorylation, hydroxylation, acylation of the terminal amino transformation of the terminal carboxyl group into an amide one group and

8. Explain the role of post-translational modifications of protein molecules: the formation of disulfide bridges, hydrolysis of peptide bonds under the action of specific proteases, glycosylation, phosphorylation / dephosphorylation, hydroxylation, acylation of the terminal amino transformation of the terminal carboxyl group into an amide one group and

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

Chapter15: From Dna To Protein

Section: Chapter Questions

Problem 4TYK

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Glycosylation is a major type of protein post-translational modification. Identify the amino acid that is joined to each monosaccharide by a glycosidic bond. glycoprotein A glycoprotein B glycoprotein C HA HO Н CH₂OH HO OH Н H CH₂OH Н ОН HO HN-C-CH3 о c=0 NHI -NH-C - CH2C-H ОН Н нн ОН НН CH2OH Он OH HO Н NH 1 С=0 -CH2-C-н NH C=0 LO-CH2-C-H NH A В с
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
9. List down the different fragments that would result if dynorphin were cleaved by trypsin. 10. How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. 11. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin.
Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn Erase
2. Compare and contrast the biological roles of the following amino acids the following pairs of amino acids. Once you have documented these role state which member of the pair is most important and why (1-2 sentences) Pair #1 Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Aspartic acid Glutamic acid Important in which pathways Pair #2 Arginine Histidine Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Pair #3 Ketogenic, glucogenic or both Prevalence in peptides and proteins Role in biosynthesis Role in homeostasis (e.g. ammonia) Important in which pathways Tyrosine Phenylalanine
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
Briefly describe each of the following possible posttranslational protein modifications. Give an example of each. Cross-linkage glycosylation and phosphorylation cleavage assembly into polymeric proteins (> 1 polypeptide)
Please ASAP. Thank you. How does the mutation change/affect the structure of the Hb heterotetramer (ie how is quaternary protein structure affected)?
Translate the given amino acid sequence into one-letter code. Glu-Leu-Val-Ile-Ser-Ile-Ser-Leu-Ile-Val-Ile-Asn-Gly-Ile-Asn-Ala-Thr-Leu-Ala-Asn-Thr-Ala Translated code: X Incorrect
6) Proteins can be modified by phosphorylation, which adds a phosphate group to the hydroxyl group of serine, threonine, or tyrosine residues. The R-group for phosphoserine is shown at right. A) The image below is an Isoelectric focusing strip that shows the unphosphorylated protein-of-interest (in blue). To which side of the unphosphorylated protein would you expect to see the phosphorylated protein? (Draw an arrow to indicate direction). Briefly justify your answer. un-phosphorylatable: Low pH Justify: B) To study the effects of phosphorylation, researchers often mutate a Ser/Thr to appear as though it is always phosphorylated or never phosphorylated at a particular site. What amino acid substitution should you use to preserve similar dimensions as Ser (or Thr) but make the side chain appear to be: constitutively (always) phosphorylated: Justify: Ser or Thr → O O=P-O O I CH₂ Ser or Thr➜ Phosphoserine High pH
Changing one amino acid within a protein sequence from a tryptophan to a stop codon would be best classified as Amino acids groups Group Characteristics Names Ala, Val, Leu, Ile, Pro, Phe Trp, Met Ala: A Leu: L non-polar hydrophobic Arg: R Asn: N Lys: K Met: M Asp: D Cys: C Gly: G polar hydrophilic (non-charged) Gly , Ser, Thr, Cys, Tyr, Asn Gln Phe: F Pro: P Ser: S acidic negatively charged Asp, Glu Glu: E Gln: Q Thr: T His: H lle: I Trp: W Туr: Y Val: V basic positively charged Lys, Arg, His A) Conservative missense O B) Nonsense O C) Neutral O D) Non-conservative missense
Which of the choices are types of posttranslational modifications a newly synth 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 Incorrect < Feedback Macmillan Learning There are four correct choices. Proteolysis (proteolytic cleavage) is the partial or complete breakdown of a protein. Keep in mind that amino acids are linked together during protein synthesis. Recall that some proteins are posttranslationally modified to form glycoproteins. Consider the structure, or components of, a glycoprotein. In addition, think about how the methylation of a protein affects intramolecular forces.