Chapter 2: Chemistry of Life
Download
Report
Transcript Chapter 2: Chemistry of Life
Name & describe the subatomic particles of an atom,
& indicate which one accounts for the
occurrence of isotopes. LT#1
Protons (+), neutrons (0), electrons (-)
p & n have mass weight of 1 amu; e- have ~ no mass
Isotopes = same atomic # but different #s of neutrons
so different mass weights
14 C*
C
*radioactive = break apart to form
6
6
smaller atoms and release radioactivity in the process –
useful in medical diagnostics (radioactive Iodine is
used to assess thyroid activity)
12 C
6
13
Distinguish between ionic & covalent reactions, &
between ionic & covalent bonds.
Ionic reactions/bonds – atoms give up or take on
electrons to achieve stability
E.g. salts NaCl
Covalent reactions/bonds – atoms share electrons to
achieve stability
E.g. molecules like proteins, lipids/fats, carbohydrates
E.g. water – bipolar – electrons are shared unevenly
List & discuss the functions of ions in the
body.
Salt = ionic bond & too much or too little is a problem
Too much = retain water & increase BP
Too little = muscle cramps, dizziness
Too much water & too little salt = water intoxication
(flu-like symptoms)
Ca2+ is needed for bone strength
K+ is needed for muscle contraction
Fe2+ is needed to transport oxygen
Describe the structure of water, & give examples
of how it functions in the body.
Water molecules are bipolar
Relatively weak H bonds allow water to be
cohesive=cling so boiling & freezing points are
extreme allowing it to be liquid at body T°
Absorbs heat before evaporating & releases heat as it
cools down (sweat cools)
Tubular vessels –
water’s shape/cohesiveness allows for
ease of transport & distribution
of substances & heat
Relate the term electrolyte to the presence
of ions in body fluids & tissues.
Electrolyte = a substance containing free ions that
make a substance electrically conductive
Electrolytes = substances that break apart and release
ions when put into water & can conduct an electric
current
Electrolyte balance is important in body fluids to
maintain health/functioning of vital organs –heart,
brain, nerve impulses, muscle contraction
Define the terms acid and base. Describe the pH
scale, & explain the significance of buffers.
Acids dissociate in water releasing hydrogen ions (H+)
in excess
Bases dissociate in water releasing hydroxide ions
(OH-) in excess (= low H+)
Water has an equal number of H+ and OH- releasing
only one of each ion (H+ = OH-)
Blood pH ~ 7.4 [<7.35 = acidosis >7.45 = alkalosis]
pH 6.9 or 7.8 is fatal!
Significance of buffers
Buffers help keep pH constant by taking up excess H+
or OH- {resist changes in pH}
Maintaining the proper pH is critical for the chemical
reactions that occur in the body. In order to maintain
the proper chemical composition inside the cells, the
chemical composition of the fluids outside the cells
must be kept relatively constant = homeostasis.
Carbonic acid – bicarbonate buffer in blood is
maintained by respiration, elimination, sweat
Compare & contrast the structures & functions of
carbohydrates, lipid, proteins, & nucleic
acids.
Carbohydrates = saccharides
Lipids = insoluble in water [NONPOLAR]
made up of fatty acids & glycerol
Proteins = amino acids
Nucleic acids = nucleotides
Carbohydrates:
structure & function
Monomer = monosaccharide (i.e. glucose)
Ring structure C6H12O6
Disaccharide = 2 monosaccharides condensed
together (maltose=glucose + glucose; sucrose = glucose
+ fructose)
Carbs are for quick energy
Polysaccharide = many monos. condensed together so
lots of E stored (glycogen in liver, starch in plants)
Lipids:
Structure & function
Carbon chains with hydrogen attached
Saturated = no double bonds – all hydrogens possible
are held
Unsaturated
= has double bonds
between Carbons
Glycerol has H-C-OH
attached to 3 Cs
Glycerol structure
Glycerol is a unit molecule of fats (along with fatty acids)
Lipid function
Long term energy storage
Membrane structure – phospoholipid bilayer
Steroids – 4 fused carbon rings – to form cholesterol
which is the building block for many other steroids
Adosterone – regulation of sodium level in blood
Sex hormones – estrogen, testosterone
Proteins
Structure & function
Kerotin – hair & nails
Collagen – connective tissue: cartilage, bone,
ligaments & tendons
Muscles – contractile proteins actin & myosin
Enzymes – organic catalysts
Amino acids are monomers and are joined together by
peptide bonds
Polymers are polypeptides with 3 levels of structures
(fig 2.13 page 28) – heat, low pH can cause unraveling
Nucleic Acids
Structure & function
Monomers are nucleotides
Nitrogen base, 5 carbon
sugar, & a phosphate
Explain what enzymes are, & describe their
role in the body.
Enzymes are protein catalysts =
speed reactions – both synthetic
and metabolic rxns
A rxn that normally would take
several hours/days without an
enzyme can take a split second.
Examples: formation of glycogen,
breakdown of foods
The seven categories of food (digestive)
enzymes and their activities are:
Amylase: breaks down
starches. (pictured)
Cellulase: breaks down fibers.
Lactase: breaks down dairy
products.
Lipase: breaks down fats.
Maltase: breaks down grains.
Protease: breaks down
proteins.
Sucrase: breaks down sugars.
Describe how the structure & function of
DNA & RNA differ.
DNA & RNA are polymers of
nucleotides
DNA – genetic code,
double strand
RNA – protein synthesis
role in conjunction with
DNA, single strand
The genes we inherit
determine the types of
proteins we can make
Describe the structure of ATP, & explain how
ATP functions in the body
Adenosine triphosphate is a nucleotide
Adenine & 3 phosphate groups = high E phosphate
bonds
Breaking phosphate bonds releases E
When cells need E they spend ATP
If ATP is $1 then cells get 36 pennies per ATP
Synthetic rxns
Active transport
Nerve impulses
Muscle contraction
ATP ADP releases E
ADP ATP requires glucose
metabolism