BIO3 Flashcards

BIO3

1
Q

What determines protein folding?

A

Favorable and unfavorable interactions influence folding energy.

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2
Q

What are intrinsically disordered proteins?

A

Proteins that lack a well-
defined structure - associated with signaling and regulatory processes.

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3
Q

What are examples of protein misfolding/aggregation diseases?

A

Examples include Alzheimer’s and Parkinson’s diseases.

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4
Q

What is allostery?

A

Process where a a molecule binds to a protein at one site, causing a change in the protein’s shape and activity at a different site.

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5
Q

What are enzymes and why are they superior to non-biological catalysts?

A

Enzymes are biological catalysts with high specificity and efficiency.

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6
Q

What is directed evolution and how is it used to improve enzymes?

A

Directed evolution is a method for evolving enzyme functionality.

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7
Q

What are antibodies and their roles in biology and applications?

A

Antibodies recognize foreign substances, essential in immunity and therapies.

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8
Q

What are nanobodies, and why are they better suited for some applications?

A

Nanobodies are smaller, more stable, and easier to produce than antibodies.

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9
Q

What is the key idea of protein display technologies like phage display?

A

Display technologies present proteins like antibodies on the surface of viruses or other platforms.

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10
Q

What is proteomics and what experimental method is it based on?

A

Proteomics studies the protein set of a cell, often via mass spectrometry.

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11
Q

Advantages and disadvantages of chemical synthesis vs recombinant production of proteins?

A

Chemical synthesis is faster, higher error rater; recombinant is more scalable more accurate folding.

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12
Q

What is self-assembly, and what is its role in biology?

A

Molecules adopt a defined arrangement without guidance. Also called “folding”.

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13
Q

Examples of sustainable sourcing of food proteins.

A

Examples include plant-based and lab-grown protein sources.

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