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
![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](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F244d6c99-1af7-41f8-abd2-7460c0e18ea6%2F53bb1259-5626-4582-af99-ba61afe8de28%2F52125o_processed.jpeg&w=3840&q=75)
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
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