Understanding Proteins and Their Structures

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28 Terms

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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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Peptide Bond

Covalent bond between amino acids in proteins.

<p>Covalent bond between amino acids in proteins.</p>
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Polypeptides

Chains of amino acids linked by peptide bonds.

<p>Chains of amino acids linked by peptide bonds.</p>
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Protein Folding

Process determining protein's 3D structure and function.

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Primary Structure

Sequence of amino acids in a polypeptide chain.

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Secondary Structure

Stable configurations like alpha helices and beta sheets.

<p>Stable configurations like alpha helices and beta sheets.</p>
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Tertiary Structure

Overall 3D shape of a protein from side chain interactions.

<p>Overall 3D shape of a protein from side chain interactions.</p>
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Quaternary Structure

Structure formed by multiple polypeptide chains.

<p>Structure formed by multiple polypeptide chains.</p>
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Essential Amino Acids

Amino acids that must be obtained through diet.

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Non-Essential Amino Acids

Amino acids synthesized by the body.

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Conditional Amino Acids

Amino acids required during specific physiological conditions.

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Protein Deficiency Malnutrition

Health issues from lack of essential amino acids.

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Hydrogen Bonds

Weak bonds crucial for protein secondary and tertiary structures.

<p>Weak bonds crucial for protein secondary and tertiary structures.</p>
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Ionic Bonds

Electrostatic attractions between charged side chains.

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Disulfide Bridges

Covalent bonds between cysteine side chains stabilizing structure.

<p>Covalent bonds between cysteine side chains stabilizing structure.</p>
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Hydrophobic Interactions

Non-polar side chains cluster to avoid water.

<p>Non-polar side chains cluster to avoid water.</p>
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Alpha Helices

Coiled structure formed in protein secondary structure.

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Beta-Pleated Sheets

Staggered strand configuration in protein secondary structure.

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Denaturation

Loss of protein structure and function due to stress.

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Optimal Temperature

Temperature at which proteins function best (~37ºC).

<p>Temperature at which proteins function best (~37ºC).</p>
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Optimal pH

pH level where proteins maintain proper structure.

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Globular Proteins

Compact proteins with functional roles in cells.

<p>Compact proteins with functional roles in cells.</p>
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Fibrous Proteins

Structural proteins providing support and strength.

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R-groups

Variable side chains that determine amino acid properties.

<p>Variable side chains that determine amino acid properties.</p>
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Hydrophilic Properties

Attraction to water, affecting protein solubility.

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Hydrophobic Properties

Repulsion from water, influencing protein folding.

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Vegan Diet Considerations

Need for careful amino acid intake to avoid deficiency.

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Chemical Diversity

Variety in R-groups leading to diverse protein functions.