General, Organic, and Biochemistry
General, Organic, and Biochemistry
9th Edition
ISBN: 9780078021541
Author: Katherine J Denniston, Joseph J Topping, Dr Danae Quirk Dorr
Publisher: McGraw-Hill Education
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Chapter 18, Problem 18.64QP
Interpretation Introduction

Interpretation:

The less elastic nature of α-keratins that have disulfide bond as compared to α-keratins without disulfide bonds has to be explained.

Concept Introduction:

The fibrous proteins such as α-keratins have helical structured polypeptide chains. These structures give support to the hair, nails, hooves, and fur of most of the animals.

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32. Consider a two-state system in which the low energy level is 300 J mol 1 and the higher energy level is 800 J mol 1, and the temperature is 300 K. Find the population of each level. Hint: Pay attention to your units. A. What is the partition function for this system? B. What are the populations of each level? Now instead, consider a system with energy levels of 0 J mol C. Now what is the partition function? D. And what are the populations of the two levels? E. Finally, repeat the second calculation at 500 K. and 500 J mol 1 at 300 K. F. What do you notice about the populations as you increase the temperature? At what temperature would you expect the states to have equal populations?
30. We will derive the forms of the molecular partition functions for atoms and molecules shortly in class, but the partition function that describes the translational and rotational motion of a homonuclear diatomic molecule is given by Itrans (V,T) = = 2πmkBT h² V grot (T) 4π²IKBT h² Where h is Planck's constant and I is molecular moment of inertia. The overall partition function is qmolec Qtrans qrot. Find the energy, enthalpy, entropy, and Helmholtz free energy for the translational and rotational modes of 1 mole of oxygen molecules and 1 mole of iodine molecules at 50 K and at 300 K and with a volume of 1 m³. Here is some useful data: Moment of inertia: I2 I 7.46 x 10- 45 kg m² 2 O2 I 1.91 x 101 -46 kg m²

Chapter 18 Solutions

General, Organic, and Biochemistry

Ch. 18.10 - How does extremely low pH cause proteins to...Ch. 18.11 - Prob. 18.11QCh. 18.11 - Prob. 18.12QCh. 18 - Prob. 18.13QPCh. 18 - Prob. 18.14QPCh. 18 - Prob. 18.15QPCh. 18 - Prob. 18.16QPCh. 18 - Prob. 18.17QPCh. 18 - Prob. 18.18QPCh. 18 - Prob. 18.19QPCh. 18 - Prob. 18.20QPCh. 18 - Prob. 18.21QPCh. 18 - Prob. 18.22QPCh. 18 - Describe the basic general structure of an...Ch. 18 - Prob. 18.24QPCh. 18 - Prob. 18.25QPCh. 18 - Prob. 18.26QPCh. 18 - Prob. 18.27QPCh. 18 - Prob. 18.28QPCh. 18 - Prob. 18.29QPCh. 18 - Prob. 18.30QPCh. 18 - Prob. 18.31QPCh. 18 - Prob. 18.33QPCh. 18 - Prob. 18.63QPCh. 18 - Prob. 18.64QPCh. 18 - Prob. 18.65QPCh. 18 - Prob. 18.66QPCh. 18 - Prob. 18.67QPCh. 18 - Prob. 18.68QPCh. 18 - Prob. 18.69QPCh. 18 - Prob. 18.70QPCh. 18 - Prob. 18.71QPCh. 18 - Prob. 18.72QPCh. 18 - Prob. 18.73QPCh. 18 - Prob. 18.74QPCh. 18 - Carbon monoxide binds tightly to the heme groups...Ch. 18 - Prob. 18.76QPCh. 18 - Prob. 18.77QPCh. 18 - Prob. 18.78QPCh. 18 - Prob. 18.79QPCh. 18 - Prob. 18.80QPCh. 18 - Prob. 18.81QPCh. 18 - Prob. 18.82QPCh. 18 - Prob. 18.85QPCh. 18 - Prob. 18.86QPCh. 18 - Prob. 18.87QPCh. 18 - Prob. 18.88QPCh. 18 - Prob. 18.89QPCh. 18 - Prob. 18.90QPCh. 18 - Prob. 18.91QPCh. 18 - Prob. 18.92QPCh. 18 - Prob. 18.93QPCh. 18 - Prob. 18.94QPCh. 18 - Prob. 18.95QPCh. 18 - Prob. 18.96QPCh. 18 - Why is it necessary to mix vegetable proteins to...Ch. 18 - Prob. 18.98QPCh. 18 - Prob. 18.99QPCh. 18 - Prob. 18.100QPCh. 18 - Calculate the length of an α-helical polypeptide...Ch. 18 - Proteins involved in transport of molecules or...Ch. 18 - The α-keratin of hair is rich in the amino acid...Ch. 18 - Calculate the number of different pentapeptides...
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