Glutamine is a conservative replacement for asparagine in the primary structure of a protein. This implies that Glutamine is a conservative replacement for asparagine in the primary smplies thatGln has a similar structure to AsnGln and Asn have the same isoelectric pointO The replacement of Asn to Gln will likely to change the structure of the proteinO The replacement of Asn to Gln will likely to destroy the function of the protein

Aspargine and glutamine are amino acids with polar side chain. They are not charged. They have amide…

Glutamine is a conservative replacement for asparagine in the primary s mplies that Gln has a similar structure to Asn O Gln and Asn have the same isoelectric point O The replacement of Asn to Gln will likely to change the structure of the protein O The replacement of Asn to Gln will likely to destroy the function of the protein

Glutamine is a conservative replacement for asparagine in the primary s mplies that Gln has a similar structure to Asn O Gln and Asn have the same isoelectric point O The replacement of Asn to Gln will likely to change the structure of the protein O The replacement of Asn to Gln will likely to destroy the function of the protein

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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A protein X is extensively methylated at lysine residues, converting it to protein Y. If the protein is to be separated by cation exchanger, what would be the order of elution? CAX, followed by Y OB. Y, followed by X OC. Both will be eluted at the same time O D. Both will bind with the matrix in the exchanger and will not elute out OE. A cation exchanger is not the ideal matrix for the separation
The peptlde bradykinln is a nonapeptlde. Give the name of the peptide (shown below) by namlng the amlno aclds from the N-terminal to the C- terminal. Use the long name, the 3-letter abbreviation and the 1-letter abbreviation. What is the pl of this peptide? Name Compositon Fxnction LOcalizatio Bradykinl Inflammatio Different n and H N vasodilation Cells HNH n Animal H. HNH H NH он HN N HO
Which of the following peptide sequences is most likely to be found in a hydrophobic pocket of the protein containing it DEAD AVGF ACMN GSYK
wnich snows tne specinicity pockets. The S pocket nas a Ra glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S,' pocket is deep and hydrophobic. Suggest a 3-amino acid sequence that this protease would R2 H cleave and indicate between which sites the peptide bond would be broken. S2 Which sequence would this protease cleave? Val-Lys-Phe Phe-Lys-Val Lys-Phe-Val Val-Phe-Lys Phe-Val-Lys O Lys-Val-Phe The peptide bond that is broken is between which sites? O S2 and S,' OS, and S,' O S2 and S1 O S2 and S1, and S and S,' IZ
The a and ß subunits of hemoglobin bear a remarkable structural similarity to myoglobin. However, certain residues that are hydrophilic in myoglobin are hydrophobic in the subunits of hemoglobin. Why might this be the case? O Hydrophilic residues on the surface of myoglobin form ionic interactions with similar regions on other myoglobin molecules. O Hydrophobic residues on the surface of hemoglobin subunits interact with similar regions on the other subunits through van der Waals interactions. Hemoglobin forms long, extended structures that feature repeated sequences, whereas myoglobin forms globular structures. Myoglobin is a water-soluble protein, whereas hemoglobin is found in the hydrophobic environment of membranes.
Which of the following polypeptides is the most hydrophobic? Val Met Pro Gly Trp lle Leu Ala Gly Met Cys Phe Trp Pro Met Phe Glu Glu Ser Ala Gly Asn Asp Met Asp Glu Asp Glu Met Glu Pro Leu Asp Asp Val Glu Asn Ser His Asn Gln Ser Thr Tyr Ala His Asp Gln Arg His Val Lys Met Lys Arg Trp Trp Lys lle His
Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere on the protein (phosphorylation). The basic reaction is: E + ATP2 Ep + ADP Po SERINE PHOSPHO SERINC (Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium between inactive and active forms conformations of the enzyme: [Eactive] [Einactive] Einactive 2 Eactive; K* The same basic equilibrium must exist for the phosphorylated protein: [Ep,active] [Ep,inactive] EP,inactive 2 Ep,active; Kp = (a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why? (b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate (e.g. the reactant whose chemistry it catalyzes)? Why or why not?
Which of the following is not correct regarding protein domains or modules such as the immunoglobulin domain, growth factor domain, and fibronectin domain? each type of domain is found in a variety of proteins O they always have the same function in differend proteins O domains are hypically 40 to 100 amine acids in length O they can be present in multiple copies in the same protein domains of a certain type usuaily have the same tertiary structure
Consider the positively charged amino acid lysine Lys2+ 21 COOH I H&N-C-H I pH 14 12 10 8 6 4 2 0 CH₂ I CH₂ I CH₂ I CH₂ T NH₂+ 0 Nelson p85 2.18 = 2.18 PK₁ Lys+ COO™ I H₂N-C-H H₂N-C-H ī I -----) 8.95 Lysº 8.95 pK₂ pka carboxyl = 2.19 pkaamino = 9.67 pka sidechain = 4.25 COO™ I CH₂ I CH₂ I CH₂ I CH₂ I NH₂¹ 1.0 2.0 Equivalents of OH added- COO™ I H₂N-C-H I 10.79 1 10.79 pk Isoelectric point Lys CH₂2 I CH₂ I CH₂ I CH₂ T NH₂ 3.0 +H3N NH3+ T CH₂ T CH₂ CH₂ CH₂ -COO™ H Lysine (Lys, K) Physiological pH = 7.4 < pl → Amino acid is positively charged at physiological pH 1. Consider glutamate in its fully protonated form (e.g. in a pH = 1 solution) 1) Draw all the forms of glutamate at various pH 2) Calculate the pl of this amino acid 3) Sketch a titration curve showing pH as a function of added [OH-] and locate the predominant forms of histidine in the curve STEPS: 1. Find the H atoms that can be removed on the molecule 2. Associated a pka value to each removable H. 3. Draw the Aa structure at:…
The figure shows interaction of various amino acids (Phe, Arg, and Asn) present in Hb with 2,3-DPG. The side chains of these amino acids and 2,3-DPG interactions are circled in red. HO Но Phe HN Asn H2N NH Arg You identify a mutant version of the globin chain where the Arg in circle 2 is replaced with aspartic acid in a patient. Would the Hb protein in this patient be able to transport oxygen even in the presence of 2,3-DPG? ASPARTIC ACID (asp) No, because the mutant Hb version will bind 2,3 DPG, and not oxygen Yes, because the mutant Hb version will bind 2,3 DPG, and not oxygen Yes, because the mutant Hb version will bind oxygen and not 2,3 DPG
Which of the following protein can be identified from the primary amino acid sequence? 15838E101 A Peripheral membrane protein B Lipid-linked protein 4585 C None of above D Integral protein
Theoretical and experimental measurements show that in many cases, thecontributions of ionic and hydrogen-bonding interactions to ΔH for proteinfolding are close to zero. Provide an explanation for this result.