Biochemistry: The Molecular Basis of Life
Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
Question
Book Icon
Chapter 11, Problem 40RQ
Summary Introduction

To review:

The mechanism by which lipoproteins transport water-insoluble lipids in the bloodstream.

Introduction:

Lipids are important, nonpolar molecules present in the body. Lipoproteins contain triacylglycerols and phospholipidsand are amphipathic in nature. The internal orientation consists of the lipophilic portion and the external orientation consists of the hydrophobic portion.

Blurred answer
Students have asked these similar questions
From the reaction data below, determine whether the reaction is first order or second order and calculate the rate constant. Time (s) 0 Reactant (mM) 5.4 1 4.6 2 3.9 3 3.2 4 2.7 5 2.3 Only a plot of In[reactant] versus t gives a straight line, so the reaction is first order . The negative of the slope, k, is 0.171
Hair grows at a rate of about 20 cm/yr. All this growth is concentrated at the base of the hair fiber, where a-keratin filaments are synthesized inside living epidermal cells and assembled into ropelike structures. Two-chan 14 Protofilament 20-30 A Two-chain Intermediate flament -Protob Protofilament Cross section of a hair The fundamental structural element of a keratin is the a helix, which has 3.6 amino acid residues per turn and a rise of 5.4 A perlum. 54A (36) Amino terminus Carbon Hydrogen Oxygen Nitrogen group Carboxyl terminus Assuming that the biosynthesis of a helical keratin chains is the rate-limiting factor in the growth of hair, calculate the rate at which peptide bonds of a-keratin chains must be synthesized (peptide bonds per second) to account for the observed yearly growth of hair. 0422 rate of peptide bond formation: Income bonds/s
Specific rotation is a measure of a solution's capacity to rotate circularly polarized light. The unfolding of the a helix of a polypeptide to a random conformation is accompanied by a large decrease in specific rotation. Polyglutamate, a polypeptide made up of only 1-Glu residues, has the a helix conformation at pH 3. When researchers raise the pH to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (1.-Lys residues) is an a helix at pH 10, but when researchers lower the pH to 7 the specific rotation also decreases, as shown in the graph. a Helix Specific rotation Poly(Glu) a Helix Random conformation Poly(Lys) Random conformation T + ° 2 4 6 В 10 12 14 PH Complete the statements about the molecular mechanism for these changes in specific rotation. Increasing the pH of a polyglutamate solution from 6 to 7 causes the carboxyl group of each glutamate residue Comed Artwer lose a proton. The negatively charged groups in each glutamate residue…

Chapter 11 Solutions

Biochemistry: The Molecular Basis of Life

Knowledge Booster
Background pattern image
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
Text book image
Curren'S Math For Meds: Dosages & Sol
Nursing
ISBN:9781305143531
Author:CURREN
Publisher:Cengage
Text book image
Biomedical Instrumentation Systems
Chemistry
ISBN:9781133478294
Author:Chatterjee
Publisher:Cengage
Text book image
Aquaculture Science
Biology
ISBN:9781133558347
Author:Parker
Publisher:Cengage
Text book image
Anatomy & Physiology
Biology
ISBN:9781938168130
Author:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble
Publisher:OpenStax College
Text book image
Human Heredity: Principles and Issues (MindTap Co...
Biology
ISBN:9781305251052
Author:Michael Cummings
Publisher:Cengage Learning
Text book image
Principles Of Pharmacology Med Assist
Biology
ISBN:9781337512442
Author:RICE
Publisher:Cengage