IB Biology: Proteins

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28 Terms

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Proteins

Biomolecules composed of amino acid chains.

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Amino Acids

Building blocks of proteins with variable side chains.

<p>Building blocks of proteins with variable side chains.</p>
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Alpha Carbon

Central carbon atom in amino acids.

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Peptide Bond

Covalent bond between amino acids' amine and carboxyl groups.

<p>Covalent bond between amino acids' amine and carboxyl groups.</p>
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Polypeptides

Chains of amino acids linked by peptide bonds.

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Essential Amino Acids

Cannot be synthesized by the body, must be ingested.

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Non-Essential Amino Acids

Can be synthesized by the body from other amino acids.

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Conditional Amino Acids

Required during specific conditions like illness or pregnancy.

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Protein Deficiency Malnutrition

Health issues from lack of essential amino acids.

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Hydrolysis Reactions

Breakdown of polypeptides into amino acids using water.

<p>Breakdown of polypeptides into amino acids using water.</p>
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Primary Structure

Sequence of amino acids in a polypeptide chain.

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Secondary Structure

Folding patterns like alpha helices and beta sheets.

<p>Folding patterns like alpha helices and beta sheets.</p>
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Alpha Helices

Coiled structure formed by hydrogen bonds in proteins.

<p>Coiled structure formed by hydrogen bonds in proteins.</p>
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Beta-Pleated Sheets

Staggered strand conformation in protein folding.

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Tertiary Structure

Three-dimensional shape of a protein determined by side chains.

<p>Three-dimensional shape of a protein determined by side chains.</p>
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Quaternary Structure

Complex of multiple polypeptide chains or prosthetic groups.

<p>Complex of multiple polypeptide chains or prosthetic groups.</p>
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Denaturation

Loss of protein structure and function due to stress.

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Hydrophobic Properties

Non-polar amino acids cluster inside globular proteins.

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Hydrophilic Properties

Polar amino acids interact with water, influencing protein function.

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Integral Proteins

Proteins embedded in cell membranes with hydrophobic regions.

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Chemical Diversity

Variety in amino acid side chains affects protein function.

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Protein Functions

Roles include structure, hormones, immunity, transport, and enzymes.

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Hydrogen Bonds

Weak bonds stabilizing protein structures like secondary and tertiary.

<p>Weak bonds stabilizing protein structures like secondary and tertiary.</p>
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Ionic Bonds

Attractions between charged side chains affecting protein shape.

<p>Attractions between charged side chains affecting protein shape.</p>
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Disulfide Bridges

Covalent bonds between cysteine residues stabilizing protein structure.

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Zwitterions

Amino acids with both positive and negative charges.

<p>Amino acids with both positive and negative charges.</p>
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Optimal pH

pH level at which a protein functions best.

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Thermal Energy

High temperatures disrupt hydrogen bonds in proteins.