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Biology > Proteins > Flashcards

Proteins Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Protein Elements

A

CHONS

Carbon, Hydrogen, Oxygen, Nitrogen, (Sometimes) Sulfur

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2
Q

Amino Acid Basic Structure

A

Amine Group

Carboxyl Group

Carbon in the middle which bonds
with Hydrogen Atom

R Group which is specific to each amino acid (20 R Groups correspond to 20 Amino Acids)

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3
Q

Condensation Reaction

A

The formation of two amino acids forming a dipeptide, but removes water to form peptide bond.

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4
Q

Hydrolysis Reaction

A

Hydrolysis breaks dipeptide down into 2 amino acids, but uses water to split

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5
Q

Difference with Essential and Non-Essential Amino Acids

A

Essential: Can not be synthesized in the body and must be included in diet

Non-Essential: Can be synthesized in the body from other amino acids

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6
Q

Elements of Carbohydrates, Fats and Proteins

A

Carbohydrates and Fats: CHO

Proteins: CHONS

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7
Q

Solubility of Carbohydrates, Fats and Proteins

A

Carbohydrates: Only sugars are soluble

Fats: Low solubility is soluble

Proteins: Some are soluble

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8
Q

Storage of Carbohydrates, Fats and Proteins

A

Carbohydrates and Fats: Can be stored

Proteins: Can’t be stored

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9
Q

Simplest Unit of Carbohydrates, Fats and Proteins

A

Carbohydrates: Monosaccharides

Fats: Fatty Acids and Triglycerides

Proteins: Amino Acids

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10
Q

Bond of Carbohydrates, Fats and Proteins

A

Carbohydrates: Glycosidic Bond

Fats: Ester Bond

Proteins: Peptide Bond

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11
Q

Origin of Carbohydrates, Fats and Proteins

A

All of them are plant

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12
Q

How many Sequences relating to Amino Acids

A

For every polypeptide with n amino acids, there are 20^n possible sequences

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13
Q

The 7 Proteins and their Functions

A

Hemoglobin: Transport

Actin and Myosin: Muscle contraction

Rubisco: Enzyme

Immunoglobulins: Immunity

Rhodopsin: Receptor

Insulin: Hormonal

Collagen: Structural

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14
Q

Denaturation

A

A permanent irreversible change in the 3D structure of a protein that results in the loss of their natural function

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15
Q

Temperature in Denaturation

A

High temperature disrupts the hydrogen bonds that hold the protein together, thus when the bonds break down the protein unfolds and loses its function

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16
Q

pH in Denaturation

A

Changing the pH affects the ionic bond between opposite charges of non-adjacent amino acids, which will alter protein shape

Changes in pH also affect the strength of the hydrogen bond

17
Q

The 4 Protein Structures

A

Primary

Secondary

Tertiary

Quaternary

18
Q

Explain Primary Protein Structure

A

A sequence of amino acids in a polypeptide molecule.

It is specific, predictable, and repeatable.

Its precision determines the 3D structure and function

19
Q

Explain Secondary Protein Structure

A

The polypeptide chains are coiled or pleated into different shapes:

Alpha Helix: A helical 3D shape

Beta-pleated Sheet: Parallel sections of polypeptide chains that run in opposite directions

20
Q

Explain Tertiary Protein Structure

A

3D because of protein folding, and is stabilized by intramolecular bonds that form between amino acids’ R groups.

Amino acids include:

Hydrogen Bonds
Disulfide Bonds
Ionic Bonds
Hydrophobic Interactions

21
Q

Explain Quaternary Protein Structure

A

Two or more polypeptide chains join to form a protein

22
Q

Difference with a Conjugated and Non-conjugated Protein

A

Conjugated: Combined an inorganic component called a prosthetic group

Non-conjugated: Made of polypeptide chain that is not associated with other chemical groups

23
Q

Fibrous Protein Features

A

Long and narrow

Structural role

Insoluble in water

Repetitive amino acid sequence

24
Q

Globular Protein Features

A

Rounded

Functional role

Soluble in water

Irregular amino acid sequence

25
Q

Hemoglobin and Function

A

Transport protein

Made of 4 polypeptide chains and has 4 heme prosthetic groups

Each heme group binds to oxygen and transports it with the red blood cell

26
Q

Rubisco and Function

A

Has a rounded shape that is tertiary, which provides three dimensional active site where a substrate can bind

The prosthetic group can be a metal ion

27
Q

Insulin and Function

A

Made of two polypeptide chains linked by disulfide bonds which is quaternary

Its shape allows it to bind to insulin receptors to regulate glucose uptake

28
Q

Collagen and Function

A

A fibrous protein made from 3 polypeptide chains held closely by covalent and hydrogen bonds to form a triple helix

Forms the main structure in tissues such as skin, blood vessels and ligaments

Quaternary

29
Q

Water Soluble Proteins

A

Non-polar amino acids tend to move towards the center of the molecule which maximizes hydrophobic interactions between amino acids to stabilize the molecule

Polar amino acids tend to move towards the protein surface which maximizes hydrogen bonding

30
Q

Membrane Bound Proteins

A

Non-polar amino acids tend to connect themselves in the membrane away from water which creates a stable environment within the membrane

Polar amino acids are found on the aqueous environment inside and outside the cell which facilities the stability of the protein

Biology (24 decks)

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