KINE 112 – Proteins Study Guide Flashcards

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A vocabulary-based flashcard set covering the chemical structure, organization, synthesis, functions, digestion, and balance of proteins based on KINE 112 lecture materials.

Last updated 5:58 AM on 6/18/26
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33 Terms

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Amino group

A functional group (represented as NH2NH_2) found in every amino acid.

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Acid group

A functional group (represented as COOHCOOH) found in every amino acid.

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Side chain (RR group)

The only part of an amino acid that differs between types and determines their specific characteristics.

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Dipeptide

A chain consisting of 2 amino acids linked together.

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Tripeptide

A chain consisting of 3 amino acids linked together.

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Polypeptide

A protein fragment containing more than 10 amino acids.

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Primary Structure

The specific sequence of amino acids in a linear chain.

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Secondary Structure

The bends and folds in a protein chain caused by chemical bonds.

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Tertiary Structure

The three-dimensional shape of a protein which determines its physiological function.

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Quaternary Structure

The interaction of two or more proteins which can activate or deactivate function.

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Essential Amino Acids

A group of 9 amino acids that the body cannot make and must be obtained from food.

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Non-Essential Amino Acids

A group of 11 amino acids that the body can synthesize from other amino acids.

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Transamination

The process through which the body synthesizes non-essential amino acids from other amino acids.

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Limiting Amino Acid

The essential amino acid in shortest supply that, when missing, causes protein synthesis to slow or stop.

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Protein Turnover

The constant process of proteins being broken down, repaired, and rebuilt.

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Edema

Swelling caused by fluid accumulation, which can occur when plasma protein levels are low.

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Buffers

Proteins that help maintain normal body pH by absorbing or releasing hydrogen ions.

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Hemoglobin

A transport protein responsible for carrying oxygen in the blood.

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Transferrin

A transport protein responsible for carrying iron in the blood.

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Lipoproteins

Proteins characterized by their function of transporting lipids.

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Gluconeogenesis

The process by which the liver converts amino acids into glucose when carbohydrate intake is low.

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Protein Energy Density

Proteins provide 4kcal/g4\,kcal/g of energy.

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Complete Proteins

Food sources that contain all 9 essential amino acids, such as meat, eggs, dairy, tofu, and quinoa.

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Incomplete Proteins

Food sources low in one or more essential amino acids, such as rice, beans, lentils, nuts, and seeds.

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Complementary Proteins

Two incomplete proteins combined (e.g., rice + beans) to provide a complete set of essential amino acids.

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Denaturation

The process where heat (cooking) or acid (HClHCl in the stomach) uncoils or softens proteins to make them easier to digest.

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Pepsin

A stomach enzyme activated by gastrin that is responsible for about 1020%10-20\% of protein digestion.

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Pancreatic Enzymes

Specific enzymes including trypsin, chymotrypsin, and carboxypeptidase that break proteins into peptides and amino acids in the small intestine.

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Nitrogen Equilibrium

A state where nitrogen intake equals nitrogen output, typical in healthy adults.

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Positive Nitrogen Balance

A state where nitrogen intake is greater than output (Nitrogen In > Nitrogen Out), occurring during growth, pregnancy, or recovery.

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Negative Nitrogen Balance

A state where nitrogen output is greater than intake (Nitrogen In < Nitrogen Out), occurring during fasting, protein deficiency, or infection.

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Adult Protein RDA

The recommended intake for healthy adults is 0.8g/kg/day0.8\,g/kg/day.

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Anaphylaxis

A severe, emergency allergic reaction causing airway swelling, drop in blood pressure, and difficulty breathing.