Identify the incorrect statement regarding the polypeptide, Myoglobin.Select one:- ○ a. The interaction between Myoglobin and O₂ is homotropic 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 O₂

Myoglobin: a. It is a monomeric protein that contains 153 amino acids. b. It has a single…

Answered: Identify the incorrect statement…

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

See similar textbooks

Similar questions

You are attempting to crystallize the head group of a myosin-like muscle protein from a newly discovered vertebrate organism. Assuming that the protein structure is similar to other vertebrate myosins, which enzymes should you use to remove the myosin-like head group from the rest of the myosin-like protein? A) both trypsin and myosinase B) both trypsin and papain C) papain D) trypsin E) myosinase
Protein-X has a calcium (Ca²+)-binding regulatory subunit. Upon calcium (Ca²+) binding the protein changes its own conformation resulting in the conformation change of protein-Y. As a result of this calcium (Ca²+)-dependent protein-X mediated conformational change protein-Y exposes the myosin II head binding sites on the skeletal muscle actin filaments. Identify the protein-X and protein-Y from the following choices. O Protein-X: Troponin; Protein-Y: Tropomysosin O Protein-X: Tropomodulin; CapZ O Protein-X: Nebulin; Protein-Y: Titin Protein-X: Tropomysosin; Protein-Y: Tropomodulin
why do transmembrane proteins cross the phospholipid bilayer as an a-helix or B-barrel? A. These structures arrange polar peptide bonds and hydrogen bonds to the exterior of the helix or barrel while nonpolar side chains are on the interior. B. These structures sequester polar peptide bonds and hydrogen bonds to the interior of the helix or barrel while nonpolar sidechains are on the exterior.
Sickle cell anemia is a horrific molecular disease that causes a multitude of issues within the human body, despite the disease’s hemoglobin only slightly varying in structure, as normal hemoglobin’s glutamic acid is instead replaced with valine in the beta-globin amino acid chain. By only changing structurally in this slight amount , sickle cell takes on its unique shape which then causes a multitude of issues within the human body. How does the replacement of glutamic acid with valine end up resulting in this shape, and how would it affect its interaction with the rest of the body?
Actin filaments have polarity. The plus end is the end to which subunits are added more rapidly, or the end of polymerization. Which of the following would enable you to identify the plus end of actin filaments? A. Adding radiolabeled actin subunits to a mixture of actin filaments in which conditions favor depolymerization B. Adding radiolabeled actin subunits to a mixture of actin filaments in which conditions are favorable for polymerization C. Determining the ionic charge of the ends of the actin filaments D. None of the above
The 2-3 phosphoglycerate (BFG) binds to the central gap formed by the hemoglobin monomers (a2b2) facilitating the reversible release of oxygen. Approximate relationships between BFG concentrations in red blood cells and Pos in hemoglobin are in the table.a) Draw the reaction schemeb) Write the forces that condition the union between hemoglobin and BFG
Microfilaments are long filamentous proteins made up of many globular proteins. What main protein are microfilaments composed of?
A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a dissociation equilibrium constant (Kd) value of 100 nM at 25°C, and the Kd remains the same at 37°C. 1) What is AS of binding at 25°C? Assume ACp of the binding is 0 over the temperature range. AS = 1.34E2 kJ/(mol*K) (note the unit!!) (sig. fig =3) 2) What is the concentration of the PL complex formed at equilibrium when you mix 0.20 uM (microM) of Protein and 1.0 uM of Ligand together at 37°C? PL at equilibrium = 8.1E-1 uM (note the unit!!) (sig. fig =2)
T/F Type I collagen fibers, that consist of collagen triple helices aligned side-by-side, are strengthened by covalent cross-links between amino acid side chains of different collagen triple helices. True O Failse
Do fungi, plants or bacteria have proteins that resemble human myoglobin?
B-mercaptoethanol is a reducing agent for disulfide bonds, resulting in the breakage of the disulfide bond. The structure of the human milk protein B-casein is unaffected when exposed to B-mercaptoethanol. What does this indicate about the composition of B-casein? Select the best option. a. B-casein has no / few cystines. b. B-casein has no / few cysteines. c. B-casein has no / few methionines. d. B-casein has no / few amino acids with chiral side chains.
The folding and unfolding rate constants for a myoglobin mutant have been determined. The unfolding rate constant ke-u = 3.62 x 10-55 and the folding rate constant ku-p = 255 s1, where Fis the folded protein and U is the unfolded (denatured) protein. For wild-type myoglobin, AG;u = +37.4 kJ/mol. Which myoglobin is more thermodynamically stable, the mutant or the wild-type?

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS