Proteins and Their Structures

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These flashcards cover key vocabulary related to proteins, their structures, and functions.

Last updated 8:25 PM on 4/4/26
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15 Terms

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Protein

Large, complex molecules made from chains of amino acids that play a role in the structure and metabolism of living organisms.

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Amino Acid

The basic building blocks of proteins, which join via peptide bonds to form polypeptides.

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Peptide Bond

The bond formed between the amino group of one amino acid and the carboxyl group of another, creating a dipeptide or polypeptide.

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Primary Structure

The linear order of amino acids in a polypeptide, determining the properties and shape of the protein.

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Secondary Structure

The way amino acids fold or twist into structures such as alpha helices or beta pleated sheets due to hydrogen bonding.

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Alpha Helix

A common secondary structure in proteins where hydrogen bonds form between amino acids, causing the chain to twist into a spiral.

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Beta Pleated Sheet

A secondary structure formed by adjacent polypeptide chains that are arranged in opposite directions, stabilized by hydrogen bonds.

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Tertiary Structure

The overall three-dimensional structure of a protein, formed by interactions between R groups of amino acids.

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Quaternary Structure

The arrangement of multiple polypeptide chains into a single functional protein.

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Denaturation

The process by which proteins lose their structure due to changes in temperature, pH, or other environmental factors, resulting in loss of function.

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Fibrous Proteins

Proteins that form long fibers or sheets; typically provide structural support and are not soluble in water.

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Globular Proteins

Proteins that are compact and soluble in water, often involved in metabolic processes.

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Hydrophobic Interaction

The tendency of non-polar R groups to orient away from water in aqueous environments, stabilizing protein structure.

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Van der Waals Forces

Weak attractions that occur between atoms that are close together, contributing to protein structure stability.

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Hydrogen Bonding

The interaction between the electronegative oxygen of a carboxyl group and the electropositive hydrogen of an amino group, important for stabilizing protein structures.

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