Chapter 19- Amino Acids and Proteins

Hematology Nurses

Specialize in blood disorder treatments.

Proteins

Polymers made from 20 different amino acids.

Functions of Proteins

Structural and functional roles in the body.

Amino Acids

Molecular building blocks of proteins.

Central Carbon Atom

Carbon bonded to functional groups in amino acids.

Ammonium Group

Functional group contributing positive charge in amino acids.

Carboxylate Group

Functional group contributing negative charge in amino acids.

R Group

Variable side chain defining amino acid characteristics.

Ionized Groups

Ammonium and carboxylate give amino acids zero charge.

Nonpolar Amino Acids

Hydrophobic amino acids with hydrogen or alkyl R groups.

Polar Amino Acids

Hydrophilic amino acids with water-interacting R groups.

Polar Neutral Amino Acids

Contain hydroxyl, thiol, or amide R groups.

Polar Acidic Amino Acids

Contain carboxylate R groups.

Polar Basic Amino Acids

Contain ammonium R groups.

Amino Acid Abbreviations

Three-letter and one-letter codes for amino acids.

Serine

Amino acid with three-letter abbreviation Ser.

Aspartate

Amino acid with three-letter abbreviation Asp.

Cystinuria

Inherited disease causing high cystine in urine.

Cystine Stones

Formed from high cystine concentration in urine.

Hemoglobin

Protein transporting oxygen in the blood.

Myoglobin

Protein storing oxygen in muscle tissues.

Physiological pH

Normal body pH affecting amino acid charge.

Classification of Amino Acids

Based on specific R group characteristics.

Cystine

Solid formed from two cysteine molecules.

Dipeptide

Peptide formed from two amino acids.

Tripeptide

Peptide formed from three amino acids.

Tetrapeptide

Peptide formed from four amino acids.

Pentapeptide

Peptide formed from five amino acids.

Polypeptide

Chain of multiple amino acids.

N-terminus

Start of a peptide, amino group present.

C-terminus

End of a peptide, carboxyl group present.

Primary Structure

Sequence of amino acids in a protein.

Thyroid Hormone

Tripeptide stimulating thyroxin release.

Insulin

First protein with determined primary structure.

Disulfide Bonds

Covalent bonds linking polypeptide chains.

Amino Acid Sequence

Specific order of amino acids in a peptide.

Condensed Structural Formula

Simplified representation of a molecule's structure.

Peptide Naming

Starts with N-terminal amino acid name.

Amino Acid Residues

Individual amino acids in a peptide chain.

Peptide Naming Convention

Replace 'ine' or 'ate' with 'yl'.

Glycylserylmethionine

Example of a tripeptide name.

Phenylalanylcystylalanine

Name of a specific tripeptide.

Biological Activity

Functionality of proteins in biological processes.

Amino Acid

Building blocks of proteins.

Peptide Formation

Process of linking amino acids via peptide bonds.

Glycylglycylalanine

Tripeptide formed from two glycines and one alanine.

Glycylalanylglycine

Tripeptide formed from one alanine and two glycines.

Alanylglycylglycine

Tripeptide formed from one alanine and two glycines.

Essential Amino Acids

Nine amino acids not synthesized by the body.

Complete Proteins

Proteins containing all essential amino acids.

Incomplete Proteins

Proteins lacking one or more essential amino acids.

Secondary Structure

Protein structure formed by hydrogen bonding.

Alpha Helix

Corkscrew shape formed by hydrogen bonds.

Beta-Pleated Sheet

Sheet-like structure formed by hydrogen bonds.

Triple Helix

Three polypeptide chains woven together for strength.

Collagen

Protein providing strength in connective tissues.

Hydrogen Bonds

Attractive forces between hydrogen and electronegative atoms.

Beta-Amyloid Proteins

Proteins involved in Alzheimer's disease pathology.

Plaques

Clusters of insoluble protein fragments in Alzheimer's.

Neurofibrillary Tangles

Aggregates of hyperphosphorylated tau protein in neurons.

Alzheimer's Disease

Dementia characterized by memory loss and plaques.

Polypeptide Chain

Chain of amino acids linked by peptide bonds.

Protein Structure

Three-dimensional arrangement of amino acids in proteins.

Peptide Bond

Covalent bond linking amino acids in proteins.

Protein Folding

Process by which a protein assumes its functional shape.

Tertiary Structure

Three-dimensional shape formed by amino acid interactions.

Quaternary Structure

Structure formed by multiple polypeptide chains.

Polypeptide Subunits

Individual chains that make up a protein.

Heme Group

Iron-containing group that binds oxygen in hemoglobin.

Hydrophobic Interactions

Attraction between nonpolar amino acid R groups.

Hydrophilic Interactions

Attraction between polar R groups and water.

Salt Bridges

Ionic attractions between polar basic and acidic R groups.

Hydrogen Bonds

Attractions between polar R groups' hydrogen and oxygen/nitrogen.

Amino Acid Residues

Building blocks of proteins, influencing structure and function.

Sickle-Cell Anemia

Condition caused by abnormal hemoglobin shape.

Glutamic Acid

Polar acidic amino acid replaced in sickle-cell anemia.

Valine

Nonpolar amino acid involved in sickle-cell anemia.

Molar Mass of Myoglobin

17,000 g/mol, lower than hemoglobin.

Molar Mass of Hemoglobin

67,000 g/mol, higher than myoglobin.

Oxygen Binding Capacity of Myoglobin

Carries one oxygen molecule.

Oxygen Binding Capacity of Hemoglobin

Carries four oxygen molecules.

Globular Protein

Protein with a compact, spherical shape.

Aqueous Environment

Water-based surroundings affecting protein interactions.

Beta Hemoglobin Chains

Subunits of hemoglobin affected in sickle-cell anemia.

Hydrophobic interactions

Cause sickle-cell hemoglobin to aggregate.

Sickle-cell hemoglobin

Forms insoluble fibers that clog capillaries.

Protein denaturation

Disruption of protein structure, rendering it inactive.

Secondary structure

Stabilized by hydrogen bonds between amino acids.

Tertiary structure

3D shape of a protein, crucial for function.

Quaternary structure

Multiple polypeptide chains forming a functional protein.

Hydrolysis reactions

Break peptide bonds to release amino acids.

Peptide bonds

Covalent bonds linking amino acids in proteins.

Amino acids

Building blocks of proteins formed by hydrolysis.

Denaturation by heat

Disrupts hydrogen bonds and hydrophobic interactions.

Denaturation by pH

Changes disrupt ionic bonds and salt bridges.

Tannic acid

Coagulates proteins to form a protective cover.

Organic compounds

Disinfectants that disrupt bacterial protein structures.

Heavy metal ions

Denature proteins by binding to ionic residues.

Mechanical agitation

Disrupts protein structure through physical stretching.

Boiling water

Denatures proteins by applying high temperature.