3.) The enthalpy change associate with a biological process is -13200 cal/mol at 298K and +14700 cal/mol at 310K. What are the values of ACp and TH? 4.) A hydrogen bond can easily form between the carbonyl (C=O) of on amino acid in a protein and a H bonded to N in another part of the protein (N-H). This is often depicted (if they are colinear as: C=O H-N but, each of these parts of the protein can also hydrogen bond to water. When the interaction above forms, we say that the Hydrogen bonds with water are exchanged for a different H- bond. Sketch the H bonds of these groups to water molecules below.

Biochemistry
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ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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### Thermodynamics and Hydrogen Bonding in Proteins

#### 3.) Enthalpy Change Calculation

The enthalpy change associated with a biological process is given as -13200 cal/mol at 298K and +14700 cal/mol at 310K. We need to determine the values of ΔCp (change in heat capacity) and T_H (the temperature at which enthalpy change is zero).

#### 4.) Hydrogen Bond Formation in Proteins

Hydrogen bonds can readily form between the carbonyl (C=O) of an amino acid within a protein and a hydrogen bonded to nitrogen (N-H) in another part of the protein. This interaction is often represented in diagrams as:

![Hydrogen Bond Diagram](diagrams.png)

- **Diagram Explanation:** This depicts a colinear orientation where a dashed line represents the hydrogen bond between the C=O group and the H-N group.

Proteins can also form hydrogen bonds with water. When the interaction between protein segments occurs, existing hydrogen bonds with water are exchanged for new protein-to-protein hydrogen bonds.

- **Exercise:** To understand this better, sketch how these protein groups (C=O and H-N) form hydrogen bonds with water molecules.

This conceptual model helps explain how proteins stabilize their structures while interacting with aqueous environments.
Transcribed Image Text:### Thermodynamics and Hydrogen Bonding in Proteins #### 3.) Enthalpy Change Calculation The enthalpy change associated with a biological process is given as -13200 cal/mol at 298K and +14700 cal/mol at 310K. We need to determine the values of ΔCp (change in heat capacity) and T_H (the temperature at which enthalpy change is zero). #### 4.) Hydrogen Bond Formation in Proteins Hydrogen bonds can readily form between the carbonyl (C=O) of an amino acid within a protein and a hydrogen bonded to nitrogen (N-H) in another part of the protein. This interaction is often represented in diagrams as: ![Hydrogen Bond Diagram](diagrams.png) - **Diagram Explanation:** This depicts a colinear orientation where a dashed line represents the hydrogen bond between the C=O group and the H-N group. Proteins can also form hydrogen bonds with water. When the interaction between protein segments occurs, existing hydrogen bonds with water are exchanged for new protein-to-protein hydrogen bonds. - **Exercise:** To understand this better, sketch how these protein groups (C=O and H-N) form hydrogen bonds with water molecules. This conceptual model helps explain how proteins stabilize their structures while interacting with aqueous environments.
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