Given the following values for 1-antitrypsin, is it likely to spontaneously adhere to the surface of the Dacron vascular graft biomaterial? Temperature = 37°C (or 410°K). Protein-related thermodynamic behavior Enthalpy (H) of proteins (related to energy) while in solution = 150 kJ/mole, and after bonding to biomaterial surface = 100 kJ/mole Entropy (S) of proteins (related to randomness) while in solution = 0.050 kJ/mole K, and after bonding to biomaterial surface = 0.025 kJ/mole K Solvent/solution-related thermodynamic behavior Enthalpy (H) of solvent/solution (related to energy) Before protein bonding to biomaterial surface = 100 kJ/mole, and after protein bonding to biomaterial surface 100 kJ/mole Entropy (S) of solvent/solution (related to randomness) Before protein bonding to biomaterial surface = 0.045 kJ/mole K, and after protein bonding to biomaterial surface = 0.037 kJ/mole@K Biomaterials-related thermodynamic behavior Enthalpy (H) of surface (related to energy) Before protein bonding to biomaterial surface = 100 kJ/mole, and after protein bonding to biomaterial surface = 150 kJ/mole Entropy (S) of surface (related to randomness) Before protein bonding to biomaterial surface = 0.005 kJ/mole K, and after protein bonding to biomaterial surface = 0.004 kJ/mole K
Given the following values for 1-antitrypsin, is it likely to spontaneously adhere to the surface of the Dacron vascular graft biomaterial? Temperature = 37°C (or 410°K). Protein-related thermodynamic behavior Enthalpy (H) of proteins (related to energy) while in solution = 150 kJ/mole, and after bonding to biomaterial surface = 100 kJ/mole Entropy (S) of proteins (related to randomness) while in solution = 0.050 kJ/mole K, and after bonding to biomaterial surface = 0.025 kJ/mole K Solvent/solution-related thermodynamic behavior Enthalpy (H) of solvent/solution (related to energy) Before protein bonding to biomaterial surface = 100 kJ/mole, and after protein bonding to biomaterial surface 100 kJ/mole Entropy (S) of solvent/solution (related to randomness) Before protein bonding to biomaterial surface = 0.045 kJ/mole K, and after protein bonding to biomaterial surface = 0.037 kJ/mole@K Biomaterials-related thermodynamic behavior Enthalpy (H) of surface (related to energy) Before protein bonding to biomaterial surface = 100 kJ/mole, and after protein bonding to biomaterial surface = 150 kJ/mole Entropy (S) of surface (related to randomness) Before protein bonding to biomaterial surface = 0.005 kJ/mole K, and after protein bonding to biomaterial surface = 0.004 kJ/mole K
Introduction to Chemical Engineering Thermodynamics
8th Edition
ISBN:9781259696527
Author:J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Publisher:J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Chapter1: Introduction
Section: Chapter Questions
Problem 1.1P
Related questions
Question
Transcribed Image Text:Given the following values for 1-antitrypsin, is it likely to spontaneously adhere to the surface
of the Dacron vascular graft biomaterial? Temperature = 37°C (or 410°K).
Protein-related thermodynamic behavior
Enthalpy (H) of proteins (related to energy)
while in solution = 150 kJ/mole, and after bonding to biomaterial surface = 100 kJ/mole
Entropy (S) of proteins (related to randomness)
while in solution = 0.050 kJ/mole?K, and after bonding to biomaterial surface = 0.025 kJ/mole@K
Solvent/solution-related thermodynamic behavior
Enthalpy (H) of solvent/solution (related to energy)
Before protein bonding to biomaterial surface = 100 kJ/mole, and after protein bonding to biomaterial
surface
100 kJ/mole
-
Entropy (S) of solvent/solution (related to randomness)
Before protein bonding to biomaterial surface
biomaterial surface = 0.037 kJ/mole?K
=
Biomaterials-related thermodynamic behavior
Enthalpy (H) of surface (related to energy)
Before protein bonding to biomaterial surface
surface: 150 kJ/mole
=
0.045 kJ/mole K, and after protein bonding to
=
100 kJ/mole, and after protein bonding to biomaterial
Entropy (S) of surface (related to randomness)
Before protein bonding to biomaterial surface = 0.005 kJ/mole K, and after protein bonding to
biomaterial surface = 0.004 kJ/mole K
Expert Solution
This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
This is a popular solution!
Trending now
This is a popular solution!
Step by step
Solved in 3 steps with 11 images
Recommended textbooks for you
Introduction to Chemical Engineering Thermodynami…
Chemical Engineering
ISBN:
9781259696527
Author:
J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Publisher:
McGraw-Hill Education
Elementary Principles of Chemical Processes, Bind…
Chemical Engineering
ISBN:
9781118431221
Author:
Richard M. Felder, Ronald W. Rousseau, Lisa G. Bullard
Publisher:
WILEY
Elements of Chemical Reaction Engineering (5th Ed…
Chemical Engineering
ISBN:
9780133887518
Author:
H. Scott Fogler
Publisher:
Prentice Hall
Introduction to Chemical Engineering Thermodynami…
Chemical Engineering
ISBN:
9781259696527
Author:
J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Publisher:
McGraw-Hill Education
Elementary Principles of Chemical Processes, Bind…
Chemical Engineering
ISBN:
9781118431221
Author:
Richard M. Felder, Ronald W. Rousseau, Lisa G. Bullard
Publisher:
WILEY
Elements of Chemical Reaction Engineering (5th Ed…
Chemical Engineering
ISBN:
9780133887518
Author:
H. Scott Fogler
Publisher:
Prentice Hall
Industrial Plastics: Theory and Applications
Chemical Engineering
ISBN:
9781285061238
Author:
Lokensgard, Erik
Publisher:
Delmar Cengage Learning
Unit Operations of Chemical Engineering
Chemical Engineering
ISBN:
9780072848236
Author:
Warren McCabe, Julian C. Smith, Peter Harriott
Publisher:
McGraw-Hill Companies, The