Biophysical Chemistry

5.

Thermodynamics of Biological Systems

5.1.

Fundamental Laws

5.1.1.

First Law of Thermodynamics

5.1.1.1.

Internal Energy

5.1.1.2.

5.1.1.3.

Conservation Principle

5.1.2.

Second Law of Thermodynamics

5.1.2.1.

Entropy Definition

5.1.2.2.

Spontaneity Criteria

5.1.2.3.

Irreversibility

5.1.3.

Third Law of Thermodynamics

5.1.3.1.

Absolute Entropy

5.1.3.2.

Zero-Point Energy

5.2.

State Functions

5.2.1.

5.2.1.1.

Definition and Measurement

5.2.1.2.

Calorimetric Determination

5.2.1.3.

Biological Applications

5.2.2.

5.2.2.1.

Statistical Definition

5.2.2.2.

Configurational Entropy

5.2.2.3.

Conformational Entropy

5.2.3.

Gibbs Free Energy

5.2.3.1.

Definition and Significance

5.2.3.2.

Standard States

5.2.3.3.

Concentration Dependence

5.2.4.

Helmholtz Free Energy

5.2.4.1.

Constant Volume Systems

5.2.4.2.

Relationship to Work

5.3.

Chemical Equilibrium

5.3.1.

Equilibrium Conditions

5.3.2.

Chemical Potential

5.3.3.

Activity and Activity Coefficients

5.3.4.

Equilibrium Constants

5.3.5.

Temperature Dependence

5.3.6.

Le Chatelier's Principle

5.4.

Biological Applications

5.4.1.

Protein Folding Thermodynamics

5.4.1.1.

Stability Measurements

5.4.1.2.

Denaturation Studies

5.4.1.3.

5.4.2.

5.4.2.1.

Binding Constants

5.4.2.2.

Thermodynamic Parameters

5.4.2.3.

Cooperativity Effects

5.4.3.

Self-Assembly Processes

5.4.3.1.

Micelle Formation

5.4.3.2.

Membrane Assembly

5.4.3.3.

Protein Aggregation

5.4.4.

Phase Transitions

5.4.4.1.

Membrane Phase Behavior

5.4.4.2.

Protein Unfolding Transitions

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6. Chemical Kinetics and Dynamics