AP bio 3.2-3.7

Carbohydrates

Only have C:H:O - 1:2:1 - or oxygen number is closer to carbon number but not exact.

Proteins

Have C:H:O:(S):N.

Lipids

Only have C:H:O:(P) - but very little oxygen - oxygen and carbon number not close at all.

Nucleic Acids

Have C:H:O:P:N.

Monomer

Small, single unit - basic building block.

Dimer

2 monomers bonded together.

Polymer

Many monomers joined together with a covalent bond.

Anabolic

Build-up reactions that are endergonic (store energy). -

Catabolic

Breakdown reactions that are exergonic (release energy). +

Dehydration Synthesis

Chemical reaction that occurs when 2 smaller molecules are joined together through covalent bonding, resulting in the formation of a larger molecule out of smaller molecules.

Hydrolysis Reaction

Chemical reaction that occurs when a larger molecule breaks down into smaller molecules by the cleaving of covalent bonds.

Monosaccharide

Monomer - single, simple sugar with a 1C:2H:1O ratio.

6-Carbon sugars

Examples include Glucose C6H12O6.

Isomers

Fructose & Galactose.

5-Carbon sugars

Examples include Ribose (C5H10O5) and Deoxyribose (C5H10O4).

Disaccharide

Dimer - double sugar.

Sucrose

Formed from Glucose + Fructose.

Polysaccharide

Polymer - complex carbs.

Glycosidic Bond

Covalent bond that holds monomers together to make polymers in sugars.

Alpha-glucose

1-hydroxyl and 4-hydroxyl on the same side.

Beta-glucose

1-hydroxyl and 4-hydroxyl on opposite sides.

Starch

Energy storage polysaccharide in plants.

Glycogen

Animal energy storage polysaccharide - short term energy storage.

Cellulose

Structural polysaccharide in plants - most abundant on Earth.

Chitin

Structural polysaccharide in animals/fungus.

Polymerization

Connection of many monomers.

Depolymerization

Break down of many polymers.

Polysaccharide Structure - Starch

Helical

Amylose

Simple starch - unbranched

Amylopectin

Complex starch - branched

Cellulose Structure

Linear with H-bonds, insoluble fiber that stimulates production of mucus.

C-H Bond

Nonpolar covalent bond - insoluble in water.

Energy Storage of Lipids

Stores energy (2 times more energy than carbs).

Adipose

Long term energy storage, insulation for warmth, cushion/protection for organs.

Fatty Acid

Carboxyl group bonded to long hydrocarbon chain.

Glycerol

3-C backbone - sugar alcohol.

Ester Linkage

Covalent bond between glycerol and fatty acid (O-C-O).

Triglyceride

Glycerol + 3 Fatty Acids.

Hydrolysis

Used to cleave covalent bonds between monomers.

Saturated Fatty Acids

All single C-C bonds - linear - maximum H, pack together tightly and solidify at room temperature.

Unsaturated Fatty Acids

Contain at least one C-C double bond, creating kinks that prevent tight packing, remaining liquid at room temperature.

Phospholipid

1 Glycerol, 2 fatty acids, and a Phosphate group, amphipathic.

Steroid

4 fused carbon rings with different functional groups attached, serving various physiological functions.

Cholesterol

The basis for forming all other steroids, provides structural stability to animal cell membranes.

Amino Acid

Monomer of proteins, 20 total differing at R Group.

Dipeptide

Dimer of amino acids.

Polypeptide

Polymer, a 'peptide chain' of amino acids.

Glycoprotein

Protein + Carbohydrate, found in cell membrane, helps with cell recognition.

Peptide Bond

Covalent bond holding amino acids together.

Amino Acids

The building blocks of proteins, containing an amino group, a carboxyl group, and a side chain (R group).

Nonpolar side chains

Hydrophobic side chains in amino acids that do not interact favorably with water.

Polar side chains

Hydrophilic side chains in amino acids that interact favorably with water.

Ionic

A type of bond formed between positively and negatively charged side chains.

Basic (positively charged) NH3+

A characteristic of basic amino acids that have a positively charged amino group.

Acidic (negatively charged) COO-

A characteristic of acidic amino acids that have a negatively charged carboxyl group.

Protein Function

The diverse roles proteins play, including enzymatic, defensive, hormonal, transport, receptor, structural, contractile, and storage functions.

Primary Structure

The linear sequence of amino acids in a protein, determined by DNA.

Secondary Structure

The folding of the polypeptide backbone stabilized by hydrogen bonds, forming alpha helices and beta pleated sheets.

Tertiary Structure

The 3D shape of a protein stabilized by interactions among side chains (R groups).

Quaternary Structure

The structure formed when multiple polypeptide chains combine to form one protein.

Denature

The process of changing a protein's shape due to breakdown of interactions, causing it to unravel and lose function.

Chaperonin

Proteins that assist in the folding of other proteins, providing a safe environment for proper folding.

Renaturation

The process of a denatured protein returning to its functional shape, which is not always possible.

Nucleotide

The monomer of nucleic acids, consisting of a pentose sugar, a phosphate group, and a nitrogen base.

Polynucleotide

A polymer made up of nucleotide monomers linked by phosphodiester bonds.

Phosphodiester Bonds

Covalent bonds that connect nucleotides in a polynucleotide chain.

ATP

A nucleotide that serves as the primary energy carrier in cells, consisting of a 5-C ribose sugar, adenine base, and three phosphate groups.

ADP

A nucleotide that consists of a 5-C ribose sugar, adenine base, and two phosphate groups, releasing energy when converted from ATP.

DNA

A double helix structure that carries genetic information, with antiparallel sugar-phosphate backbones.

RNA

A single-stranded nucleic acid involved in protein synthesis, using ribose sugar and uracil instead of thymine.

Evolutionary Relationship

The concept that more similarities in DNA/protein sequences indicate a closer evolutionary relationship and a common ancestor.