Ch 5 - Pt 2 - Proteins Flashcards

0
Q

Enzyme

A

Proteins that serve as catalysts in living organisms; typically very large molecules that bring together/break apart substrates (the molecules upon which a chemical reaction occurs).

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1
Q

Catalyst

A

A substance that accelerates the rate if a chemical reaction without affecting the products of the reaction and without itself being altered or consumed by the reaction.

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2
Q

Amino acids

A

An organic molecule possessing both an amino acid and a carboxyl group.

The monomer building blocks of proteins.

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3
Q

Polypeptides

A

Polymers of amino acids

A protein consists of one or more polypeptides

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4
Q

Amino acid monomers

A

Organic molecules possessing both carboxyl and amino groups. Differ in their properties due to differing side chains (R-groups).

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5
Q

How many different amino acid monomers from which polypeptides are assembled?

A

20

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6
Q

Peptide bonds

A

The covalent bond between the carboxyl group of one amino acid and the amino group on another formed by a dehydration reaction.

The link between amino acids.

Dehydration reaction.

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7
Q

How are peptide bonds formed?

A

Through dehydration reactions.

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8
Q

How does a protein’s specific conformation/3D shape effect it’s function?

A

A protein’s specific conformation determines its function

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9
Q

What are some examples of models depicting a proteins specific conformation (3D shape)?

A

Space-filling model, ribbon model, 3D complementarity between an antibody protein and an invading virus particle

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10
Q

What are the 4 levels in protein structure?

A

Primary, secondary, tertiary, and (in some cases) quaternary structure

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11
Q

Primary structure of a protein

A

1) The linked series of amino acids with a unique sequence.
2) The 29 amino acids can be assembled into 20^127 sequences.
3) Primary structure dictates structure at higher levels.

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12
Q

Secondary structure of proteins

A

Hydrogen bonds between amino acids of a single polypeptide (a helix) or amino acids of adjacent polypeptides (B sheet) bring about secondary structure

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13
Q

Tertiary structure if proteins

A

1) Results from interactions between the side chains (R-groups) of amino acids
2) Involves a variety of bonds: disulfide bridges, hydrogen bonds, van der Waals interactions, ionic bonds

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14
Q

Quaternary structure of proteins

A

Are comprised of 1+ polypeptide subunits

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15
Q

Example of the importance of primary structure

A

Sickle-cell hemoglobin differs from normal hemoglobin in only one amino acid

16
Q

Denaturation

A

Occurs when a protein unravels and loses its 3D confirmation

Ex: cooking meat, ceviche

17
Q

Protein functions

A

Enzymes, structural proteins, storage proteins, transport proteins, hormones, receptor proteins, contractile and motor proteins, defensive proteins

18
Q

Structural proteins

A

Keratin: structural protein in hair, nails, etc
Collagen: the most abundant protein in animals and provides the high tensile strength and resilience in skin, tendons, and ligaments

19
Q

Storage proteins

A

Ovalbumin (albumin): egg white is 10% protein dissolved in water and serves as a source of nutrition for a developing embryo

20
Q

Hormone (proteins)

A

Insulin: a protein hormone produced in the pancreas; regulates carbohydrate metabolism

21
Q

Receptor proteins

A

Transmembrane receptor proteins can pump molecules against their diffusion gradient and are also involved in promoting and regulating chemical reactions in cells

22
Q

Contractile and motor proteins

A

Dynein: the motor protein that moves material within the cell by “walking” along support structures in cells

23
Q

Defensive proteins

A

Antibodies are protein signals and binding sites for components of the immune system.
(Ex: the venom of stingrays)

24
Q

Protein

A

A biologically functional molecule that consists of one or more polypeptides, each folded and coiled into a 3D structure