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.

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