lecture 6 thermo Flashcards

1
Q

For a spontaneous reaction delta G must be what?

A

<0 (-VE) (less than 0)

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2
Q

For a spontaneous reaction delta G must be what?

A

<0 (-VE) (less than 0)

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3
Q

What does > mean?

A

> is a symbol that means “greater than

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4
Q

What does < mean?

A
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5
Q

For determining values that will give a spontaneous reaction what needs to be done?

A

Find T where DeltaG = 0 then any T greater than that value will give a spontaneous reaction

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6
Q

What is isothermal titration calorimetry? (ITC)

A

Excellent for studying biomolecular interactions between for example protein-small molecules, protein-protein, target drugs, enzyme exhibitors, and protein-DNA. ITC directly measures the heat released or absorbed during a biomolecular binding event.

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7
Q

What is Differential Scanning Calorimetry? DSC?

A

Used to investigate the stability of biological (and other) systems. Measures the enthalpy of unfolding due to denaturation and the change in heat capacity of denuration.

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8
Q

What are heat capacity changes associated with protein unfolding due to?

A

Changes in the hydration of side chains that were buried in the native state, but become solvent exposed in the denatured state.

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9
Q

What does > mean?

A

> is a symbol that means “greater than

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10
Q

What does < mean?

A
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11
Q

For determining values that will give a spontaneous reaction what needs to be done?

A

Find T where DeltaG = 0 then any T greater than that value will give a spontaneous reaction

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12
Q

What is isothermal titration calorimetry? (ITC)

A

Excellent for studying biomolecular interactions between for example protein-small molecules, protein-protein, target drugs, enzyme exhibitors, and protein-DNA. ITC directly measures the heat released or absorbed during a biomolecular binding event.

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13
Q

What is Differential Scanning Calorimetry? DSC?

A

Used to investigate the stability of biological (and other) systems. Measures the enthalpy of unfolding due to denaturation and the change in heat capacity of denuration.

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14
Q

What are heat capacity changes associated with protein unfolding due to?

A

Changes in the hydration of side chains that were buried in the native state, but become solvent exposed in the denatured state.

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