Proteins (Unit 1) Flashcards

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1
Q

Proteins

A

Polymer of many amino acids folded into a 3D structure that specifies its region

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2
Q

Protein Functions

A

Catalyze chemical reactions, provide structural support, Transport substances, Regulate cell processes, Provide defence from disease

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3
Q

Amino Acids

A

Building blocks of proteins

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4
Q

Components of amino acids

A

Amino group and carboxyl group

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5
Q

Types of amino acids

A

20 different acids - 12 natural, 8 essential. Can be polar (R contains N,O,S), nonpolar (R contains only C) or carry a charge

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6
Q

Structure of Proteins

A

Primary, Secondary, Tertiary, Quaternary

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7
Q

Primary Structure

A

Peptide Chain. AA are joined by peptide linkages through condensation. Hydroxyl of carboxyl and hydrogen from amino is lost.

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8
Q

Secondary Structure

A

H Bonds between carbonyl of one bond and amino of other. Can form alpha helix (spiral) or beta pleated sheet (layers)

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9
Q

Tertiary Structure

A

Protein folding is due to/stabilized by intermolecular interactions between side chains of amino acids. Disulphide bonds can form with two sulfhydryl groups. H-bonds, Hydrophilic, and Hydrophobic, all influence group location during folding. Salt bridge

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10
Q

Salt Bridge

A

Electrostatic attractions between electrically charged amino acid side chains

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11
Q

Quaternary Structures

A

Occurs if more than 2 polypeptides make up protein. Join through intermolecular, and sometimes covalent interactions

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12
Q

Denaturation

A

Intermolecular forces in proteins are broken, so will lose shape and stop performing functions

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13
Q

Causes of Denaturation

A

Temperature, pH, chemicals

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