Macromolecules

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162 Terms

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Monosaccharide

One carbohydrate unit

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Disaccharide

Two carbohydrate units linked together

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Oligosaccharide

Three to ten carbohydrate units linked together

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Polysaccharide

More than ten carbohydrate units linked together

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Fischer Projection

Represents the carbohydrate molecule in a straight-chain configuration

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Haworth Projection

Represents the cyclical structure of a carbohydrate molecule

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Chair Conformation

A chair-like representation of the most stable conformation of a carbohydrate molecule

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D- and L-isomers

Molecules with the same chemical components but are mirror images of each other

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Dextrorotatory

Molecules that rotate light to the right

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Levorotatory

Molecules that rotate light to the left

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Pyranose

A six-membered carbohydrate ring

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Furanose

A five-membered carbohydrate ring

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α-anomer

The hydroxyl group (-OH) in C1 is positioned downward

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β-anomer

The hydroxyl group (-OH) in C1 is positioned upward

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Aldose

Carbohydrate molecule with an aldehyde group at its C1

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Ketose

Carbohydrate molecule with a ketone group at its C2

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Glycoside

A carbohydrate molecule that has its hydroxyl group (-OH) bonded to another compound

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Deoxy Sugars

Sugars where oxygen is removed, such as deoxyribose found in DNA

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Amylose

A helical, non-branching polysaccharide composed of glucose units

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Amylopectin

A polysaccharide with both α(1→4) and α(1→6) glycosidic bonds, forming a branched structure

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Glycogen

A highly branched polysaccharide composed of glucose units, used for energy storage in humans

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Cellulose

A polysaccharide that makes up plant cell walls, composed of β-D-glucopyranose units

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Inulin

A polysaccharide of fructose found in tubers and roots of plants, used to assess kidney function

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Chitin

A polysaccharide that forms the exoskeletons of insects, crustaceans, and fungi

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Glycosaminoglycan

Complex carbohydrates containing amino sugars and uronic acids, which may form proteoglycans

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Hyaluronic Acid

A glycosaminoglycan found in joints, helping with lubrication

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Chondroitin Sulfate

A glycosaminoglycan that lubricates joints and reinforces cartilage

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Heparin

A naturally occurring anticoagulant found in the liver

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Glycoproteins

Proteins that contain oligosaccharide chains, important for cell recognition and communication

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ABO Blood Group Antigens

Carbohydrate chains on glycoproteins that determine blood type and are synthesized by glycosyltransferases

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Glycosyltransferase

Enzymes that add sugar molecules to proteins or lipids, playing a role in blood group antigen synthesis

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Lipids
Nonpolar heterogeneous group of compounds such as fats, oils, steroids, and waxes
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Simple Lipids
Esters of fatty acids with various alcohols
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Compound Lipids
Esters of fatty acids that have alcohol and possess additional groups
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Derived Lipids
Formed from hydrolysis of both simple and complex lipids
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Delta (Δ) Nomenclature
Indicates the position of double bonds in a fatty acid relative to the carboxyl (COOH) end of the molecule
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Omega (ω) Nomenclature
Indicates the position of double bonds relative to the methyl (CH3) end of the fatty acid
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Saturated Fatty Acids
Fatty acids that contain only single C−C bonds and have high melting points, being solid at room temperature
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Unsaturated Fatty Acids
Fatty acids that contain one or more double C=C bonds and have low melting points, being liquid at room temperature
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Cis Double Bond
Acyl chains are on the same side of the bond, resulting in kinks that make the fatty acid more fluid
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Trans Double Bond
Acyl chains are on opposite sides of the bond, making the fatty acid more rigid and similar to saturated fatty acids
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Triglycerides
Lipids composed of three fatty acid chains attached to a glycerol backbone
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Phospholipids
Lipids containing a phosphate group, glycerol, and two fatty acids, with amphipathic properties
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Cholesterol
A sterol compound consisting of four fused hydrocarbon rings, important for cell membrane structure and as a precursor for steroid hormones
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Eicosanoids
Chemical messengers derived from 20-carbon polyenoic fatty acids, including prostaglandins, thromboxanes, and leukotrienes
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Prostaglandins
Eicosanoids that act as local hormones and are involved in inflammation and blood flow regulation
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Thromboxanes
Eicosanoids involved in blood clotting and vascular constriction
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Leukotrienes
Eicosanoids that cause bronchoconstriction and play a role in asthma
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Lipoxins
Eicosanoids similar to leukotrienes but with four conjugated double bonds
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Glycolipids
Lipids attached to carbohydrates, often functioning as receptors or recognition sites on cell membranes
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Sphingolipids
Lipids with a sphingosine backbone and fatty acid residues attached via amide linkage, important in cell signaling and membrane structure
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Phosphoglycerides
Phospholipids that contain glycerol as the backbone and a phosphate group
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Sphingomyelins
Sphingolipids found in the myelin sheath of nerve cells, important for electrical insulation
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Cardiolipin
Phospholipid found in the mitochondria, essential for mitochondrial function
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Lysophosphatidylcholine
A component of phospholipid metabolism, involved in the interconversion of phospholipids
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Plasmalogens
Phospholipids involved in membrane structure and cell signaling, suggested to have protective effects against oxidative stress
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Steroids
Nonpolar, asymmetric molecules synthesized from cholesterol that function as hormones and other important signaling molecules
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Cholesteryl Esters
Esterified form of cholesterol found in plasma, more hydrophobic than non-esterified cholesterol
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Ergosterol
A sterol found in fungal membranes and a precursor for Vitamin D2 synthesis upon UV exposure
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Terpenes
Hydrocarbon compounds with a formula of C5H8, present in both animals and plants, with various medicinal uses
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Carotenoids
Tetraterpenoids with antioxidant and anti-inflammatory properties, including lycopene, found in various fruits and vegetables
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Lycopene
A non-provitamin A carotenoid responsible for the red color in tomatoes, linked to reduced cardiovascular disease risk
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Neutral Lipids
Lipids such as triglycerides and cholesterol that are uncharged and nonpolar
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Amino Acids
Hydrocarbons containing an amino group (NH2) and a carboxyl group (COOH) attached to an α-carbon
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Polypeptides
Chains of amino acids linked by peptide bonds
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Proteins
Linear polymers of amino acids that perform diverse functions in living systems
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Zwitterion
Molecule with both a positive and a negative charge, typically at physiological pH
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Alpha Carbon (α-carbon)
Central carbon in an amino acid to which the amino group, carboxyl group, hydrogen, and side chain (R group) are attached
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Essential Amino Acids
Amino acids that cannot be synthesized by the body and must be obtained from dietary sources
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Nonessential Amino Acids
Amino acids that can be synthesized by the body
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Peptide Bond
Covalent bond linking the amino group of one amino acid to the carboxyl group of another, formed through a dehydration reaction
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Hydrophobic Interactions
Interaction between nonpolar side chains of amino acids that tend to cluster away from water
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Disulfide Bonds
Covalent bonds formed between the thiol groups of cysteine residues, stabilizing protein structure
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Isoelectric Point (pI)
The pH at which an amino acid has no net charge, the sum of positive and negative charges is equal
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Chiral
Molecules that are asymmetric and exist as enantiomers, like amino acids, except for glycine
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D- and L-isomers
Two enantiomers of amino acids that are mirror images of each other
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Ketogenic Amino Acids
Amino acids whose catabolic products are ketone bodies like acetoacetate or acetyl-CoA
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Glucogenic Amino Acids
Amino acids that can be converted into glucose through gluconeogenesis
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Selenocysteine
A variant of cysteine where sulfur is replaced by selenium, found in certain enzymes with antioxidant activity
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Amino Acid Side Chains
The unique functional groups attached to the α-carbon that determine the chemical properties of amino acids
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Nonpolar Side Chains
Amino acids with side chains that are hydrophobic and do not participate in hydrogen or ionic bonds
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Polar Side Chains
Amino acids with side chains that are hydrophilic and can participate in hydrogen bonding
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Acidic Amino Acids
Amino acids with side chains that are negatively charged at physiological pH, such as aspartic acid and glutamic acid
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Basic Amino Acids
Amino acids with positively charged side chains at physiological pH, such as lysine, arginine, and histidine
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Peptide Bond Formation
A dehydration reaction where an amino group from one amino acid bonds with a carboxyl group of another, releasing water
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Protein Folding
The process by which a polypeptide chain folds into its functional three-dimensional structure
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Primary Protein Structure
The linear sequence of amino acids in a polypeptide chain
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Secondary Protein Structure
The localized folding of a polypeptide chain into structures such as alpha helices and beta sheets, stabilized by hydrogen bonds
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Tertiary Protein Structure
The three-dimensional arrangement of all atoms in a protein, influenced by side chain interactions
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Quaternary Protein Structure
The interaction between two or more polypeptide chains to form a functional protein
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Fibrous Proteins
Long, thin proteins that provide structural support, such as collagen and keratin
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Globular Proteins
Proteins that fold into spherical shapes and are soluble in water, like enzymes and antibodies
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Amino Acid Isomers
D- and L-forms of amino acids, with L-forms being predominantly used in proteins
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Hydrogen Bonds
Weak bonds that form between the hydrogen atom of one molecule and an electronegative atom (like oxygen or nitrogen) of another
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Alpha-Helix
A secondary structure of proteins where the polypeptide chain coils into a right-handed spiral, stabilized by hydrogen bonds
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Beta-Sheets
A secondary structure of proteins where the polypeptide chain folds into pleated sheets, stabilized by hydrogen bonds
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Peptide Bond

Rigid, planar, with partial double bond character, and typically in the trans configuration
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Amphoteric Amino Acids
Amino acids that can act as both acids and bases, depending on the pH of the environment
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Henderson-Hasselbalch Equation
Equation that relates pH, pKa, and the concentrations of an acid and its conjugate base, useful for understanding buffer capacity
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Amino Acid Catabolism
The process of breaking down amino acids to remove the α-amino group and convert the carbon skeleton into various metabolic intermediates