DAT Bootcamp Biology
Exam
2026
Master Exam Prep Bundle
(Verified Questions & Answers)
A+ Grade Guaranteed
,Matter anything that takes up space and has mass
Element a pure substance that has specific physical/chemical properties and can't be broken
down into a simpler substance
Atom the smallest unit of matter that still retains the chemical properties of the element
Molecule two or more atoms joined together
Intramolecular forces attractive forces that act on atoms within a molecule
Intermolecular forces forces that exist between molecules and affect physical properties of the substance
Monomers single molecules that can potentially polyermize
Polymers substances made up of many monomers joined together in chains
Carbohydrates - Contain carbon, hydrogen, and oxygen atoms (CHO)
Ex: Monosaccharides, disaccharides, polysaccharides
Monosaccharides carbohydrate monomers
- empirical formula: (CH2O)n.
- "n" represents number of carbons
Ribose five carbon monosaccharide
Fructose and Glucose six carbon monosaccharide
- isomers of each other (same chemical formula, different arrangement of atoms)
Disaccharides two monosaccharides joined together by a glycosidic bond
- Result of dehydration (condensation) reaction
Dehydration (condensation) reaction where a water molecule leaves and a covalent bond forms
Hydrolysis reaction a covalent bond is broken by the addition of water
2026
,Sucrose disaccharide made of glucose + fructose
Lactose disaccharide made of galactose + glucose
Maltose disaccharide made of glucose + glucose
Polysaccharides contain multiple monosaccharides connected by glycosidic bonds to form long
polymers
Starch form of energy storage for plants and is an alpha (α) bonded polysaccharide
- Linear starch: amylose
- Branched form: amylopectin
Glycogen form of energy storage in animals and is an alpha (α) bonded polysaccharide
- much more branching than starch
Cellulose structural component in plant cell walls, and is a beta (β) bonded polysaccharide
- Linear strands packed rigidly in parallel
Chitin structural component in fungi cell walls and insect exoskeletons, and is a beta (β)
bonded polysaccharide with nitrogen added to each monomer
Proteins contain carbon, hydrogen, oxygen, and nitrogen atoms (CHON)
- atoms combine to form amino acids, which link together to build polypeptides (or
proteins)
Proteome all the proteins expressed by one type of cell under one set of conditions
Amino acids monomers of proteins
- twenty different kinds of amino acids, each with a different "R-group"
Polypeptides polymers of amino acids and are joined together by peptide bonds through
dehydration reactions
- hydrolysis reactions break peptide bonds
- becomes an amino acid chain that contains two end terminals on opposite sides
N-terminus (amino terminus) the side that ends with the last amino acid's amino group of a polypeptide
C-terminus (carboxyl terminus) the side that ends with the last amino acid's carboxyl group of a polypeptide
Conjugated proteins proteins that are composed of amino acids and non-protein components
- Metalloproteins (ex: hemoglobin)
- Glycoprotein (ex: mucin)
2026
, Metalloproteins proteins that contain a metal ion cofactor
Ex: hemoglobin
Glycoprotein proteins that contain a carbohydrate group
Ex: mucin
Primary structure sequence of amino acids connected through peptide bonds
Secondary structure intermolecular forces between the polypeptide backbone (not R-groups_ due to
hydrogen bonding
- Forms α-helices or β-pleated sheets.
Tertiary structure three dimensional structure due to interactions between R-groups
- create hydrophobic interactions based on the R-groups
- disulfide bonds are created by covalent bonding between the R-groups of two
cysteine amino acids
- hydrogen bonding and ionic bonding between R groups also hold together the
tertiary structure
Quaternary structure multiple polypeptide chains come together to form one protein
Protein denaturation describes the loss of protein function and higher order structures
- only the primary structure is unaffected
Proteins will denature as a result of... high or low temperatures, pH changes, and salt concentrations
Storage (protein function) reserve of amino acids
Hormones (protein function) signaling molecules that regulate physiological processes
Receptors (protein function) proteins in cell membranes which bind to signal molecules
Structure (protein function) provide strength and support to tissues (hair, spider silk)
Immunity (protein function) antibodies that protect against foreign substances
Enzymes (protein function) regulate rate of chemical reactions
- act as biological catalysts by binding to substrates (reactants) and converting them
into products
- most enzymes are proteins
2026
Exam
2026
Master Exam Prep Bundle
(Verified Questions & Answers)
A+ Grade Guaranteed
,Matter anything that takes up space and has mass
Element a pure substance that has specific physical/chemical properties and can't be broken
down into a simpler substance
Atom the smallest unit of matter that still retains the chemical properties of the element
Molecule two or more atoms joined together
Intramolecular forces attractive forces that act on atoms within a molecule
Intermolecular forces forces that exist between molecules and affect physical properties of the substance
Monomers single molecules that can potentially polyermize
Polymers substances made up of many monomers joined together in chains
Carbohydrates - Contain carbon, hydrogen, and oxygen atoms (CHO)
Ex: Monosaccharides, disaccharides, polysaccharides
Monosaccharides carbohydrate monomers
- empirical formula: (CH2O)n.
- "n" represents number of carbons
Ribose five carbon monosaccharide
Fructose and Glucose six carbon monosaccharide
- isomers of each other (same chemical formula, different arrangement of atoms)
Disaccharides two monosaccharides joined together by a glycosidic bond
- Result of dehydration (condensation) reaction
Dehydration (condensation) reaction where a water molecule leaves and a covalent bond forms
Hydrolysis reaction a covalent bond is broken by the addition of water
2026
,Sucrose disaccharide made of glucose + fructose
Lactose disaccharide made of galactose + glucose
Maltose disaccharide made of glucose + glucose
Polysaccharides contain multiple monosaccharides connected by glycosidic bonds to form long
polymers
Starch form of energy storage for plants and is an alpha (α) bonded polysaccharide
- Linear starch: amylose
- Branched form: amylopectin
Glycogen form of energy storage in animals and is an alpha (α) bonded polysaccharide
- much more branching than starch
Cellulose structural component in plant cell walls, and is a beta (β) bonded polysaccharide
- Linear strands packed rigidly in parallel
Chitin structural component in fungi cell walls and insect exoskeletons, and is a beta (β)
bonded polysaccharide with nitrogen added to each monomer
Proteins contain carbon, hydrogen, oxygen, and nitrogen atoms (CHON)
- atoms combine to form amino acids, which link together to build polypeptides (or
proteins)
Proteome all the proteins expressed by one type of cell under one set of conditions
Amino acids monomers of proteins
- twenty different kinds of amino acids, each with a different "R-group"
Polypeptides polymers of amino acids and are joined together by peptide bonds through
dehydration reactions
- hydrolysis reactions break peptide bonds
- becomes an amino acid chain that contains two end terminals on opposite sides
N-terminus (amino terminus) the side that ends with the last amino acid's amino group of a polypeptide
C-terminus (carboxyl terminus) the side that ends with the last amino acid's carboxyl group of a polypeptide
Conjugated proteins proteins that are composed of amino acids and non-protein components
- Metalloproteins (ex: hemoglobin)
- Glycoprotein (ex: mucin)
2026
, Metalloproteins proteins that contain a metal ion cofactor
Ex: hemoglobin
Glycoprotein proteins that contain a carbohydrate group
Ex: mucin
Primary structure sequence of amino acids connected through peptide bonds
Secondary structure intermolecular forces between the polypeptide backbone (not R-groups_ due to
hydrogen bonding
- Forms α-helices or β-pleated sheets.
Tertiary structure three dimensional structure due to interactions between R-groups
- create hydrophobic interactions based on the R-groups
- disulfide bonds are created by covalent bonding between the R-groups of two
cysteine amino acids
- hydrogen bonding and ionic bonding between R groups also hold together the
tertiary structure
Quaternary structure multiple polypeptide chains come together to form one protein
Protein denaturation describes the loss of protein function and higher order structures
- only the primary structure is unaffected
Proteins will denature as a result of... high or low temperatures, pH changes, and salt concentrations
Storage (protein function) reserve of amino acids
Hormones (protein function) signaling molecules that regulate physiological processes
Receptors (protein function) proteins in cell membranes which bind to signal molecules
Structure (protein function) provide strength and support to tissues (hair, spider silk)
Immunity (protein function) antibodies that protect against foreign substances
Enzymes (protein function) regulate rate of chemical reactions
- act as biological catalysts by binding to substrates (reactants) and converting them
into products
- most enzymes are proteins
2026
