BIOLOGY 151 Study Guide - Final Guide: Covalent Bond, Hydrogen Bond, Protein Folding
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FINAL EXAM: BIO 151
BIOLOGICAL MOLECULES AND CELL THEORY
● 4 basic biological molecules:
○ Protein
■ Action molecules in the cell
■ Monomer: amino acid
■ Other molecules that are “polar” like to interact with water
● Polar molecules dissolve in water b/c they form hydrogen bonds
● Nonpolar molecules group together in water b/c the water
molecules form hydrogen bonds with one another
■ Every amino acid has an amino group, a carboxyl group, and an R group
■ The peptide bond is a covalent bond between one amino acid’s carboxyl
group and another’s amino group
■ Protein Folding: when a cytosolic protein folds, it hids the hydrophobic
amino acids inside and so the hydrophilic ones are on the outside
■ Structural, regulatory, contractile, protective; can serve in transport,
storage, or membranes
● Enzymes: produced by living cells; are catalysts in biochemical
reactions
○ Can function to break molecular bonds/rearrange
bonds/form new bonds
■ Hormones: chemical signaling molecules (proteins/steroids) secreted by
an endocrine gland that controls specific processes like growth,
development, metabolism, reproduction
■ Denaturation: loss of function and can be caused by permanent changes in
shape of protein
■ Amino acids: monomers that make up proteins
● Central carbon atom bonded to an amino group (-NH2), a carboxyl
group (-COOH) and a hydrogen atom
○ Has another variable atom bonded to the central carbon
atom (R group)
■ R group determines the chemical nature of the
amino acid w/in its protein (basic, acidic, polar,
nonpolar)
● sequence/number of amino acids determine a protein’s shape, size,
function
● Attached to another amino acid by a covalent bond (peptide bond)
● Polypeptide: polymer of amino acids
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■ The sequence for every protein is determined by the gene that encodes it
● Change in the gene sequence can lead to a different amino acid
being added to the polypeptide chain
● In the B-pleated sheets, the “pleats” are formed by hydrogen
bonding between atoms on the backbone of the polypeptide chain
○ Pleated segments align parallel to each other and hydrogen
bonds form between the same pairs of atoms on each of the
aligned amino acids
● Tertiary structure is caused by chemical interactions between
various amino acids and regions of the polypeptide
○ Interactions among the R groups create the 3D structure
○ When protein folding occurs, the hydrophobic R groups of
the nonpolar amino acids are on the inside of the protein
while the hydrophilic R groups are on the outside
○ 3-D folding pattern of a protein due to side chain
interactions
● Secondary protein structure: hydrogen bonding of the peptide
backbone causes the amino acids to fold into a repeating pattern
● Quaternary protein structure: more than one amino acid chain
● Example of denaturation: the albumin protein in the liquid egg
white when placed in a hot pan and changes from a clear substance
to an opaque white substance
○ Nucleic acids
■ A small piece of DNA is being transcribed into mRNA by polymerase
■ Transfer information and energy
■ Polymer is a nucleic acid
● Information storage, order of bases acts as a code, instructions for
making proteins
■ Charges help to interact with H2O
■ DNA: genetic material found in all living organisms, from single celled-
bacteria to multicellular mammals
■ RNA: protein synthesis; used to communicate with the rest of the cell
■ Nucleotides: monomers that make up DNA/RNA
● Nitrogenous base, a pentose (5 carbon) sugar, and a phosphate
group
○ Carbohydrates
■ Store energy and act in identification
■ Transporting potential energy
■ Some are soluble/insoluble
■ Provide energy to the body (through glucose which is a simple sugar)
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■ Monosaccharides: simple sugars (common is glucose)
● # of carbon atoms ~3-6
● -ose
■ Photosynthesis: plants synthesize glucose using co2 and water by this
■ Disaccharides: form when 2 monosaccharides goes through dehydration
reaction
● (-OH) of a monosaccharide combines w/ a hydrogen atom of
another mono. While releasing a molecule of h2o and forming a
covalent bond between atoms in the 2 sugar molecules
■ Polysaccharide: long chain of monosaccharides linked by a covalent bond
● Starch: stored form of sugars in plants and is made up of amylose
and amylopectin
● Where excess starch is stored
● Glycogen: storage form of glucose in humans/ other vertebrates
and made up of monomers of glucose
○ It’s the animal version of starch stored in liver and muscle
cells
● Cellulose: natural biopolymers; makes up the walls of plants
○ Cellulose passing through our digestive system is dietary
fiber
■ Chitin: nitrogenous carb; made of repeating units of modified sugar
containing nitrogen
○ Lipids/phospholipids
■ Energy storage and structural
■ Has a nonpolar tail and polar head group
■ Hydrophobic bc they’re nonpolar molecules
■ Hydrocarbons that include only nonpolar carbon-carbon
■ Provide insulation from environment for plants and animals
■ Fats, oils, waxes, phospholipids, steroids
■ Fat: ex. Triglyceride consists of glycerol and fatty acids
● Glycerol: organic compound w/ 3 carbon atoms, 5 hydrogen
atoms, 3 -OH groups
● Triglycerides: 3 fatty acids
● Saturated fatty acid: saturated w/ hydrogen/single bonds/packed
tightly together and are solid at room temp
● Unsaturated fatty acid: when the hydrocarbon chain contains a
double bond
○ It can help improve blood cholesterol levels
● Omega-3 fatty acids are important in brain function and normal
growth/development
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Document Summary
Other molecules that are polar like to interact with water. Polar molecules dissolve in water b/c they form hydrogen bonds. Nonpolar molecules group together in water b/c the water molecules form hydrogen bonds with one another. Every amino acid has an amino group, a carboxyl group, and an r group. The peptide bond is a covalent bond between one amino acid"s carboxyl group and another"s amino group. Protein folding: when a cytosolic protein folds, it hids the hydrophobic amino acids inside and so the hydrophilic ones are on the outside. Structural, regulatory, contractile, protective; can serve in transport, storage, or membranes. Enzymes: produced by living cells; are catalysts in biochemical reactions. Can function to break molecular bonds/rearrange bonds/form new bonds. Hormones: chemical signaling molecules (proteins/steroids) secreted by an endocrine gland that controls specific processes like growth, development, metabolism, reproduction. Denaturation: loss of function and can be caused by permanent changes in shape of protein.