Proteins Flashcards

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1
Q

What are proteins composed of?

A

Proteins are comprised of long chains of recurring monomers called amino acids

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2
Q

What is the structure of a generalised amino acid? (5 components) Draw the structure

A

Amino acids all share a common basic structure, with a central carbon atom bound to:

An amine group (NH2)
A carboxylic acid group (COOH)
A hydrogen atom (H)
A variable side chain (R)

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3
Q

How many different amino acids are there?

A

There are 20 different amino acids which are universal to all living organisms

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4
Q

How are proteins created?

A

Amino acids are joined together on the ribosome to form long chains called polypeptides, which make up proteins

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5
Q

How do amino acids differ?

A

Each type of amino acid differs in the composition of the variable side chain

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6
Q

Why do the side chains affect the type of protein?

A

These side chains will have distinct chemical properties (e.g. charged, non-polar, etc.) and hence cause the protein to fold and function differently according to its specific position within the polypeptide chain

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7
Q

How can amino acids be joined together to form a protein?

A

Amino acids can be covalently joined together in a condensation reaction to form a dipeptide bond

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8
Q

What is the covalent bond between amino acids is called?

A

The covalent bond between the amino acids is called a peptide bond

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9
Q

What are long chains of amino acids called?

A

long chains of covalently bonded amino acids are called polypeptides

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10
Q

How can polypeptide chains be broken down?

A

Polypeptide chains can be broken down via hydrolysis reactions, which requires water to reverse the process

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11
Q

What is the primary structure?

A

The order of the amino acid sequence is called the primary structure and determines the way the chain will fold

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12
Q

Do all amino acids fold the same? Why?

A

NO
Different amino acid sequences will fold into different configurations due to the chemical properties of the variable side chains

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13
Q

What two types of secondary structures are there?

A

Alpha helices

Beta-pleated sheets

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14
Q

When do amino acids fold in alpha-helices?

A

Alpha helices occur when the amino acid sequence folds into a coil/spiral arrangement

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15
Q

When do amino acids fold into beta-pleated sheets?

A

Beta-pleated sheets occur when the amino acid sequence adopts a directionally-oriented staggered strand conformation

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16
Q

What is tertiary structure?

A

The overall three-dimensional configuration of the protein casued by the R-groups ineracting to form new bonds

17
Q

What determines the tertiary structure of a protein?

A

The tertiary structure of a polypeptide chain will be determined by the interactions between the variable side chains

18
Q

What are examples of interactions of side chains which result in a tertiary structure?

A

These interactions may include hydrogen bonds, disulphide bridges, ionic interactions, polar associations, etc.

19
Q

What is Quaternary structure?

A

Arrangement and interaction of two or more polypeptide chains to form a functional protein. Each subunit is a fully folded polypeptide (from the tertiary structure).

20
Q

What is conjugated or nonconjugated?

A

Conjugated proteins have a prosthetic group (e.g., hemoglobin with heme). Non-conjugated proteins are made only of amino acids (e.g., albumin).

21
Q

Insulin

A

Type of Protein: Globular protein
Structure: Quaternary structure (two polypeptide chains held together by disulfide bonds).
Function: Regulates blood sugar levels by signaling cells to absorb glucose.

22
Q

Collagen

A

Type of Protein: Fibrous protein
Structure: Tertiary structure for individual chains, and quaternary structure for the triple helix.
Function: Provides structural support to tissues like skin, tendons, and bone

23
Q

Glycoprotein A and B solubility

A

Glycoproteins called A and B are embedded in the phospholipid bilayer where the non-polar(hydrophobic) amino acid are folded so it can interact with the hydrophobic layer of the membrane to remain embedded.

24
Q

Denaturation

A

The process where a protein loses its shape and, therefore, its function.
Cause: Heat, pH changes, or chemicals can disrupt bonds (e.g., hydrogen bonds, disulfide bridges).