Sickling occurs in deoxyhemoglobin S but not in oxyhemoglobin S. Oxyhemoglobin has a small, hydrophobic pocket in a ßchain region located in the interior of the protein. In deoxyhemoglobin, however, this pocket is located on the surface of theprotein. In deoxyhemoglobin S, Val 6 interacts with this surface pocket, leading to aggregation of HbS.Choose two amino acids that would be reasonable candidates for the pocket-Val 6 interaction.argininephenylalanineglutamateleucineserine Which amino acids would be expected to produce a similar sickling effect if substituted for Val at position 6?alanineleucinelysineargininephenylalanine

Sickling is the process where the haemoglobin protein inside the RBC cell clumps together this…

Answered: Sickling occurs in deoxyhemoglobin S…

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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Most animals cannot use wool for nourishment. An exception is the clothes moth: it can derive nourishment from eating clothing made of natural fibers such as wool (which is rich in a-keratin). The digestive tract of the larvae of clothes moths provides a highly reducing environment. Why is this beneficial to the larvae? The reducing environment will reduce the disulfide linkages, making it easier to digest the proteins. The reducing environment will hydrolyze the peptide bonds. The reducing environment will interfere with the H-bonding between the tropocollagen molecules, making the type of protein found in most natural fibres easier to digest. The reducing environment will help to kill bacterial pathogens. The reducing environment will detoxify the carcinogenic dyes used in the textile industry.
You have digested a small protein with two different proteases, each protease acting on the protein in separate reactions. These are the peptide fragments generated: Trypsin: IPVK: Ile-Pro-Val-Lys ALEL: Ala-Leu-Glu-Leu HRPGDR: His-Arg-Pro-Gly-Asp-Arg FGADAEDGAMNK: Phe-Gly-Ala-Asp-Ala-Glu-Asp-Gly-Ala-Met-Asn-Lys YLEFISECIIQVLQSK: Tyr-Leu-Glu-Phe-Ile-Ser-Glu-Cys-Ile-Ile-Gln-Val-Leu-Gln-Ser-Lys Chymotrypsin: (Reaction conditions were used to maximize cutting to the C-terminal size of F, W, and Y.) LEF: Leu-Glu-Phe IPVKY: Ile-Pro-Val-Lys-Tyr GADAEDGAMNKALEL: Gly-Ala-Asp-Ala-Glu-Asp-Gly-Ala-Met-Asn-Lys-Ala-Leu-Glu-Leu ISECIIQVLQSKHRPGDRF: Ile-Ser-Glu-Cys-Ile-Ile-Gln-Val-Leu-Gln-Ser-Lys-His-Arg-Pro-Gly-Asp-Arg-Phe I am not sure what these questions are asking.
Mutations in the ribosomal protein gene RPS19 have been found to be associated with Diamond-Blackfan anemia (DBA), a rare syndrome that disrupts erythropoiesis, the process by which new red blood cells are produced. Which of the following provides the most likely explanation for the connection between a mutation in RPS19 and a disruption in erythropoiesis? A B с D The ribosomes in the cell are unable to package and transfer the components that are required for erythropoiesis. The ribosomes in the cell are unable to facilitate the movement of nutrients that are re- quired for erythropoiesis across the cell membrane. The ribosomes in the cell are unable to correctly synthesize the proteins that are re- sponsible for erythropoiesis. The ribosomes in the cell are unable to effectively produce the ATP that is required for erythropoiesis.
List 4 different actiated carrier molecules, for each one, list both the oxided and reduced forms
The amide hydrogen atoms of peptide bonds within proteins can exchange with protons in the solvent. In general, amide hydrogen atoms in buried regions of proteins and protein complexes exchange more slowly than those on the solvent-accessible surface do. Determination of these rates can be used to explore the proteinfolding reaction, probe the tertiary structure of proteins, and identify the regions of protein–protein interfaces. These exchange reactions can be followed by studying the behavior of the protein in solvent that has been labeled with deuterium ( ²H), a stable isotope of hydrogen. What two methods described in this chapter could be readily applied to the study of hydrogen– deuterium exchange rates in proteins?
Is the whole protein (destined for the ER) synthesized and then moved to the ER or is it synthesized partially and then completed at the ER? Please explain.
Why does the dissociation constant change for hemoglobin in high and low 02 concentrations? O Hemoglobin is a tetramer and subunits have decreased dissociation of 02 when a neighboring subunit has bound 02 O Hemoglobin is a monomeric protein with increased dissociation of 02 when a neighboring molecule has bound 02 O Hemoglobin is a tetramer and subunits have increased dissociation of 02 when a neighboring subunit has bound CO O Hemoglobin is a tetramer and subunits have increased dissociation of O2 when a neighboring subunit has bound O2
4)
Identify the incorrect statement regarding the polypeptide, Myoglobin. Select one: a. The interaction between Myoglobin and O2 is homotopic in nature as indicated by a Hill coefficient n = : 1 b. Myoglobin is found predominantly in muscle tissue because it facilitates oxygen diffusion. c. The majority of Myoglobin's secondary structure is composed of alpha-helices d. Myoglobin has a higher affinity for oxygen than Hemoglobin e. Myoglobin serves as an oxygen storage protein as suggested by its hyperbolic binding of 02
The T state of hemoglobin is converted to the R state by what event? Select one: The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. а. b. None of these. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. С. d. The binding of oxygen stabilizes a more planar heme ring which alters the position of the proximal histidine and subsequently, residues between the alß2 interface. The binding of oxygen destabilizes a more planar heme ring which alters the position of the proximal proline and subsequently, residues between the alß2 interface. е.
Classify the symmetrical arrangement ofthe subunits (e.g., C2 , C3 , D 2 , helical, icosahedral). 1. Proteobacterial nitrite sensor (3PNS):2. Pseudomonad oligosaccharide receptor (7POR):3. Adenoviral structural protein (8ASP)

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