Lehninger Principles Of Biochemistry 7e & Study Guide And Solutions Manual For Lehninger Principles Of Biochemistry 7e
Lehninger Principles Of Biochemistry 7e & Study Guide And Solutions Manual For Lehninger Principles Of Biochemistry 7e
7th Edition
ISBN: 9781319125776
Author: David L. Nelson, Michael M. Cox
Publisher: W. H. Freeman
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Chapter 6, Problem 15P
Summary Introduction

To determine: The values of Km and Vmax for the given enzyme by using graphical representation.

Introduction:

Enzyme contains an active site, a region of enzyme where substrate gets binds with the active site of enzyme. After binding of enzyme with substrate, enzyme-substrate complex is formed and initiates rate of chemical reaction.

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The carbon-nitrogen peptide bond is rigid, but rotation can take place about the bond between the nitrogen and α-carbon atoms and the bond between the α-carbon and the carbonyl carbon atom. These bond angles define the conformation of the peptide chain. Consider the Ramachandran plot shown to answer both questions. (degrees) 180 120 60 60 0 Which observation most likely describes part of an observed a helix? p=-59 degrees; = +150 degrees; many Ser residues cp-140 degrees; w = +130 degrees; many Val residues op-57 degrees; w = -47 degrees; many Pro residues op-60 degrees; y = -47 degrees; many Ala residues p = +60 degrees; y = +40 degrees; many Gly residues -60 -120 -180 -180 0 ➜ (degrees) 180
The α 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? Hemoglobin forms long, extended structures that feature repeated sequences, whereas myoglobin forms globular structures. Hydrophobic residues on the surface of hemoglobin subunits interact with similar regions on the other subunits through van der Waals interactions. Hydrophilic residues on the surface of myoglobin form ionic interactions with similar regions on other myoglobin molecules. Myoglobin is a water-soluble protein, whereas hemoglobin is found in the hydrophobic environment of membranes.
Protein disulfide isomerase (PDI) is a protein folding enzyme that catalyzes disulfide-sulfhydryl exchange reactions. Ribonuclease is an enzyme with two ẞ-sheets, three α-helices, and four disulfide bridges critical to the stability of its structure. PDI rapidly converts inactive, scrambled ribonuclease to enzymatically active ribonuclease. This process is driven by the decrease in free energy as the scrambled conformations are converted into the stable, active conformation of the enzyme. In contrast, PDI rapidly inactivates insulin. What does PDI's effect on insulin imply about the structure of insulin? The three-dimensional shape of insulin does not contain any disulfide bonds. The active conformation of insulin has more ẞ-sheets than α-helices. The active conformation of insulin is not the most thermodynamically preferred form. The amino acid sequence of insulin is similar to the amino acid sequence of ribonuclease.
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License