Chapter 2: Chemistry Comes Alive (Marieb)
Chapter 2: Chemistry Comes Alive (Marieb)
Chapter 2: Chemistry Comes Alive (Marieb)
Matter is anything that occupies space and has massstates of matter are solid, liquid, and gas.
Energy
Energy is defined as the capacity to do work.
Kinetic energy energy in action
Potential energy stored energy; inactive energy that has potential
Forms of energy:
1. Chemical energy form stored in the bonds of chemical substances
2. Electrical energy results from movement of charged particles
3. Mechanical energy energy directly involved in moving matter; legs moving pedals of
bike
4. Radiant energy/electromagnetic energy energy that travels in waves
Energy can be converted but some of the energy is lost into an unusable form of energy.
Example: Electrical energy is converted to light energy in a light bulb but some energy is lost to
heat (why light bulbs become hot).
Similarly all energy conversion on the body liberate heathelping to maintain our body temp
and ensuring that chemical reactions occur (chemical reactions are more likely to happen in
increased temps).
* Carbon, oxygen, hydrogen, and nitrogen make up about 96% of the bodys weight.
Atoms all elements are composed of these more or less identical particles or building blocks;
composed of nucleus and subatomic particles
Elections orbit around the nucleus, and the orbital model depicts the probable regions of
greatest electron density by density shading
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Isotopes nearly all know elements have two or more structural variations, which have the same
number of protons and electrons but different numbers of neutrons
Identifying Elements
Atomic number equal to the number of protons in the nucleus
Mass number sum of the masses of the atoms protons and neutrons
Atomic weight average of the relative weights of all isotopes of the element, taking into
account their relative abundance in nature
Radioisotopes
Radioisotopes results when heavier isotopes of many elements are unstable and their atoms
decompose spontaneously into more stable forms in a process called radioactivity.
May be compared to tiny explosions; occurs when subatomic alpha particles or
gamma rays are ejected from the atomic nucleus
o The glue that holds even smaller particles that make of the nuclear
particles like protons, quarks, together are weaker in heavier isotopes, and
when radioisotopes disintegrate, the element may transform into different
elements.
Used in imagining
Ionizing radiation does not damage organic molecules directly. Instead, it
knocks electrons out of other atoms and sends them flying. It is the electron
energy and the unstable molecules left behind that do the damage.
Compound when two or more different kinds of atoms bind; many molecules together, such as
water (compound), which is composed of numerous H2O molecules
Mixtures
Mixtures substance composed of two or more components physically intermixed.
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Types of mixtures:
Compounds and mixtures are different because no chemical bonding occurs between
components of mixtures.
Chemical Bonds
Electron shells electrons forming the election cloud around the nucleus of an atom occupy
these regions of space
Each electron shell represents a different energy level as the attraction between the
positively charged nucleus and negative electrons is greatest when electrons are closet to
the nucleus and falls off with increasing distance, explaining why outer shell elections:
o Have the greatest potential energy (took more energy for them to overcome
nuclear attraction and reach the distant levels)
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o Are most likely interact chemically with other atoms (least tightly held by their
own atomic nucleus and more easily influenced by other atoms)
Shells hold different numbers of electrons - Shell 1 holds 2 elections; shell 2, 8 electrons;
shell 3, 18 electrons; etc.
Chemically inert some atoms are unreactive due to their being stable; occurs to atoms
with they are filled to capacity in outer shell or have 8 electrons
Valence electrons atoms outermost shell or the portion of it containing electrons that
are chemically reactive; only up 8 atoms in the outermost shell are chemically reactive
Atoms which the outermost energy level contains fewer than eight electrons tend to gain, lose, or
share electrons with other atoms to achieve stability
Chemical Bonds
1. Ionic bonds - chemical bond between atoms formed by the transfer of 1 or more
electrons from 1 atom to another, making one (or more) atoms positively charged with
the other one (or more) atoms negatively charged; the bond forms when the two charges
attract/come together
a. Anion - atom that gains the electron; net negative charge
b. Cation loses electron; net positive charge
c. Bond usually forms with atoms with 1 or 2 valence electrons and atoms with
seven shell electrons
2. Covalent bonds bonds that share electrons between all atoms; can be single, double, or
triple bonds
a. Electronegativity small atoms with six or seven valence shell electrons are
electron-hungry and attract electrons very strongly
b. Electropositive atoms with only one or two valance electrons; their electron-
attracting ability is so low that they usually lose their valance electrons
c. Types:
i. Nonpolar molecules when electrons are shared and are electrically
balanced; typically the atoms are bonded into a straight line
ii. Polar molecules when electrons are shared but not equally and thus are
not electrically balanced; usually caused by the molecules shape, with
bonds formed at definite angles
1. Creates dipoles molecule with negative charge on one end and
positive on another
3. Hydrogen bonds an attraction formed when a hydrogen atom already linked with a
electronegative atom (which makes the H end have a positive end) is attracted by another
electronegative atom
a. Gives water its high heat capacity and high heat vaporization and what makes it a
universal solvent (polar nature of molecules attracts and breaks apart other
compounds)
Chemical Reactions
Chemical reactions occurs whenever chemical bonds are formed, rearranged, or broken.
Reactants the number and kinds of reacting substances
Products the results chemical composition
H + H H2
Types:
1. Synthesis or combination reaction synthesis reaction when atoms or molecules
combine to form a large, more complex molecule
a. Anabolic constructive reactions
b. A + B AB
2. Decomposition reactions occurs when a molecule is broken down into smaller
molecules or its constituent atoms
a. Catabolic degradative
b. AB A + B
3. Exchange or displacement reactions involve both synthesis and decomposition;
reactants change partners so to speak
a. AB + C AC + B or AB + CD AD + BC
4. Oxidation-reduction reactions special type of exchange reaction because electrons are
exchanged between the reactants; basis of all reactions in which food fuels are broken
down for energy
a. Electron donor reactant that loses the electron and is oxidized
b. Electron acceptor reactant that takes up the transferred electrons and is said to
become reduced
c. Occurs when ionic compounds are formed
d. Does not always involve the complete transfer of electrons; some simply change
the pattern of electron sharing in covalent bonds
Inorganic Compounds
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Water
High heat capacity absorbs lots of heat without changing temperature
High heat of evaporation high amounts of heat is absorbed in water before it
evaporates, causing the heat to be liberated and body to cool
Polar solvent properties polar h2o molecules easily break apart other molecules by
having negative and positive parts
Reactivity reactions require water in body
Cushioning provide cushion around body organs
Salts
Ionic compound containing cations other than H+ and anions other than the hydroxyl ion
(OH-). It dissociates easily because the ions are already formed.
Electrolytes ionic substances that conduct an electrical current in solution
Bases bitter taste, feel slippery, and are proton acceptorstake up hydrogen ions (H+) in
detectable amounts
When bases dissolve in water, they release cations such as hydroxyl ions (OH-), which
then binds to a proton present in the solution, producing water and reducing the acidity of
the solution. (Water is neutral.)
Example:
NaOH Na+ + OH-
OH- + H+ H2O
o Strong bases dissociate easily in water and quickly tie up H+ ions
o Weak bases do not dissociate easily in water
Bicarbanate ion (HCO3-) important base in the body, particularly abundant in blood
Ammonia (NH3) common waste product of protein breakdown in the body is also a
base; has pair of unshared electrons that strongly attract protons. By accepting a proton,
ammonia becomes an ammonia ion
At pH 7, the number of H+ and OH- ions are the same. This is why water (made up of
chemically bonded H and OH) is neutral.
Neutralization reaction displacement reaction that occurs when acids and bases are
mixed to form water and a salt
Buffers chemical systems that work with kidneys and lungs to carefully regulate the
homeostasis of acid-base balance
Resists abrupt and large swings in the pH of body fluids by releasing hydrogen ions
(acting as acids) when the pH begin to rise and by binding hydrogen ions (acting as
bases) when the pH drops
Helps maintain homeostatic of blood through carbonic acid-bicarbonate system and
others. Carbonic acid (H2CO3) dissociates reversibly, release bicarbonate ions (HCO3-)
and protons (H+). Carbonic acid dissociates in response to rise in pH, comes back
together in response to decrease in pH.
Organic Compounds
Organic compounds all contain carbon; for most part organic molecules are large molecules
but interactions with other molecules typically involve only small, reactive parts of their
structure called functional groups (acid groups, amines, and others).
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Carbon (1) no other small atom is so electroneutral, meaning it never gains or loess lections
but instead always shares them (2) it can form four covalent bonds with other elements, allowing
them to form long, chainlike molecules, ring structures, and many other structures
Carbohydrates
Carbohydrates are a group of molecules that includes sugars and starches; contains hydrogen,
carbon, and oxygen with hydrogen and oxygen in a 2:1 ratio like water.
Carbohydrate = hydrated carbon
Functions:
o To provide a ready, easily used source of cellular fuel
When glucose is broken down and oxidized within cells, electrons are
transferred, releasing the bond energy stored in glucose. That energy is
used to synthesize ATP.
Anything left over no used to synthesize ATP is converted to glycogen or
fat and stored.
o Structural purposes (only small amount) such as some sugars found in our genes
Types:
Example:
2C6H12O6 C12H22O11 + H2O
Lipids
Lipids are insoluble in water but dissolve readily in other lipids and in organic solvents such as
alcohol and ether.
Contains carbon, oxygen, and hydrogen but with oxygen in much lower doses than with
carbohydrates. Phosphorus can be found in some of the more complex lipids.
Types:
1. Triglycerides neutral fats; commonly know as fats when solid or oils when liquid
a. Composed of two types of building blocks in 3:1 ratio:
i. Fatty acids linear chains of carbon and hydrogen with an organic acid
group (--COOH) at one end
ii. Glycerol Modified simple sugar (sugar alcohol)
b. Three fatty acid chains synthesize with a single glycerol molecule by dehydration
synthesis to result in an E-shaped moleculeglycerol backbone is always the
same b the fatty acid chains vary, which results in different kinds of fats and oils
c. Are large molecules that must be broken down into building blocks before they
can be absorbed
d. Triglycerides are nonpolar molecules because of the hydrocarbon chains
e. Most efficient and compact form of stored energy
f. Length and degree of saturation determine how solid the molecule is at a given
temp:
i. Saturated fatty acids only a single covalent bond between carbon
atoms; are straight chains and at room temp, they are packed closely
together, forming a solid
ii. Unsaturated fatty acids contains one (monosaturated) or more
(polysaturated) double bonds between carbon atoms; double bonds cause
fatty acids to kink so they cannot be packed closely enough to solidify;
are oils at room temp and are typical of plant lipids
iii. Trans fats have been solidified by addition of H atoms at sites of carbon
double bonds
2. Phospholipids modified triglycerides; are diglycerides with a phosphorus-containing
and two, rather than three, fatty acid chains
a. Phosphorus group gives phospholipids their distinctive chemical propertiesthe
hydrocarbon portion (tail) of the molecule is nonpolar and interacts only with
nonpolar molecules, but the phosphorus-containing part is polar and attracts other
polar or charged particles, such as water or ions
b. Chief material for building cellular membranes
3. Steroids basically flat molecules made of four interlocking hydrocarbon rings; fat
soluble, contain little oxygen
a. Most important one is cholesterol found in cell membranes and is the raw
material for synthesis of vitamin D, steroid hormones, and bile salts
4. Eicosanoids diverse lipids chiefly derived from a 20-carbon fatty acid found in all cell
membranes
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Proteins
Composes 10-30% of cell mass and is the basic structural material of the body; also plays vital
roles in cell functions including as enzymes, in the hemoglobin of blood, etc.
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Amino acids building blocks of proteins; 20 common types, which allows for numerous
distinct combinations and properties for resulting proteins
o Two important functional groups:
A basic group called an amine group (--NH2)
An organic acid group (--COOH)
o All amino acids are the same except for their R group, and it is the R group which
makes the amino acid unique
o Makes proteins by joining chains of amino acids together with dehydration
synthesis, with the amine end of one amino acid linked to the acid end of the other
amino acidmust have more than 50 amino acids in the chain to be a protein
Resulting bond produced peptide bonds characteristic arrangement of
linked atoms
Structural Levels:
1. Primary structure linear sequence of amino acids composing the polypeptide chain
2. Secondary structure spirals (alpha helixes), which is formed by coiling of the primary
chain and is stabilized by H bonds formed between NH and CO groups in amino acids in
the primary chain, OR pleated form (beta sheet), primary polypeptide chain are linked
side by side by H bonds to form pleated, ribbon-like structuresboth forms can be
exhibited in the same chain
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Classifications:
Proteins are classified according to their overall appearance and shape as either
Fibrous - also known as structural proteins, are extended and strandlike, soluble in
water, and very stable. Some exhibit only secondary structure, but most have tertiary or
even quaternary structure
o Provides mechanical support and tensile strength to the bodys tissues.
o Examples: collagen (single most abundant protein in the body), keratin, elastin,
and certain contractile proteins of muscle
Or globular - also called functional proteins, are compact, spherical proteins that have
tertiary structure or quaternary structure; are water-soluble, chemically active molecules
o Play crucial roles in virtually all biological processes as antibiotics, protein based
hormones, and enzymes, etc.
Classification According To
Overall
General Function Examples From the Body
Structure
Fibrous
Structural Collagen, found in all connective tissues, is the single most abundant
framework/mechanical protein in the body. It is responsible for the tensile strength of bones,
support tendons, and ligaments.
Keratin is the structural protein of hair and nails and a water-resistant
material of skin.
Elastin is found, along with collagen, where durability and flexibility are
needed, such as in the ligaments that bind bones together.
Spectrin internally reinforces and stabilizes the plasma membrane of some
cells, particularly red blood cells. Dystrophin reinforces and stabilizes the
plasma membrane of muscle cells. Titin helps organize the intracellular
structure of muscle cells and accounts for the elasticity of skeletal muscles.
Actin and myosin, contractile proteins, are found in substantial amounts in
muscle cells, where they cause muscle cell shortening (contraction); they
Movement
also function in cell division in all cell types. Actin is important in
intracellular transport, particularly in nerve cells.
Globular
Protein enzymes are essential to virtually every biochemical reaction in the
body; they increase the rates of chemical reactions by at least a millionfold.
Catalysis
Examples include salivary amylase (in saliva), which catalyzes the
breakdown of starch, and oxidase enzymes, which act to oxidize food fuels.
Hemoglobin transports oxygen in blood, and lipoproteins transport lipids
and cholesterol. Other transport proteins in the blood carry iron, hormones,
Transport
or other substances. Some globular proteins in plasma membranes are
involved in membrane transport (as carriers or channels).
Regulation of pH Many plasma proteins, such as albumin, function reversibly as acids or
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Classification According To
Overall
General Function Examples From the Body
Structure
bases, thus acting as buffers to prevent wide swings in blood pH.
Peptide and protein hormones help to regulate metabolic activity, growth,
Regulation of metabolism and development. For example, growth hormone is an anabolic hormone
necessary for optimal growth; insulin helps regulate blood sugar levels.
Antibodies (immunoglobulins) are specialized proteins released by immune
Body defense cells that recognize and inactivate foreign substances (bacteria, toxins, some
viruses).
Complement proteins, which circulate in blood, enhance both immune and
inflammatory responses.
Molecular chaperones, originally called heat shock proteins, aid folding
of new proteins in both healthy and damaged cells and transport of metal
Protein management
ions into and within the cell. They also promote breakdown of damaged
proteins.
Denatured proteins proteins can become denatured when the fragile hydrogen bonds are
broken by chemical and physical factors, such as excessive acidity or temperature, causing
proteins to unfold and lose their specific 3D shape
Often denatured proteins can regain its native structure when desired conditions are
restored but sometimes if the structure is damaged beyond repair, the protein is
irreversibly denatured.
Enzymes - globular proteins that act as biological catalysts, which are substances that regulate
and accelerate the rate of biochemical reactions but are not used up or changed in those reactions
Determines not only which reactions will be speeded up, but also which reactions will
occur.
Composition:
o Some enzymes are purely protein.
o Others consists of two parts collectively known as holoenzyme:
Apoenzyme (the protein portion)
Cofactor - depending on the enzyme, the cofactor may be an ion of a
metal element or an organic molecule.
Most organic cofactors are derived from vitamins (especially the B
complex vitamins). This type of cofactor is more precisely called a
coenzyme.
Each enzyme is chemically specific; may control a single chemical reaction or exhibit a
broader specificity in that they can bind with molecules that differ slightly and thus
regulate a small group of related reactions.
Part of the enzyme where catalytic activity occurs:
o Active site - presence of specific arrangements of atoms on the surfaces
o Substrate substance on which an enzyme acts
How Enzymes work:
o Every chemical reaction requires that a certain amount of energy, called
activation energy, be absorbed to alter the bonds of the reactants so its at an
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energy level where their random collisions are forceful enough to ensure
interaction.
Enzymes allow reactions to occur at normal body temperature by
decreasing the amount of activation energy required.
o Three steps:
1. Substrate(s) bind to the enzymes active site, temporarily forming an
enzyme-substrate complex. Causes active site to change shape so that the
substrate and active site fit together precisely.
2. The enzyme-substrate complex undergoes internal rearrangements that
form the product(s).
3. The enzyme releases the product(s) of the reaction.
DNA or deoxyribonucleic acid typically found in the nucleus of the cell; constitutes the
genetic material and
Two functional roles:
o Replicates (reproduces) itself before a cell divides, ensuring that the genetic
information in the descendant cells is identical
o Provides the basic instructions for building every protein in the body
Composed of:
o Bases in DNA are A,G, C, and T
Complementary bases bases that always bond together
A binds with T; C binds with G
o Pentose sugar is deoxyribose
Structure is a long, double-stranded polymer, which is a double chain of nucleotides,
which all forms into a spiral structure called a double helix
o Its two nucleotide chains are held together by hydrogen bonds between the bases,
so that a ladderlike molecule is formed. Alternating sugar and phosphate
components of each chain form the backbones or uprights of the ladder, and
the joined bases form the rungs.
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RNA or ribonucleic acid - located chiefly outside the nucleus and can be considered a
molecular slave of DNA
Carries out the orders for protein synthesis issued by DNA
Three major varieties/duties:
o messenger RNA
o ribosomal RNA
o transfer RNA
The amount of energy released and transferred during ATP hydrolysis corresponds closely to
that needed to drive most biochemical reactions. As a result, cells are protected from excessive
energy release that might be damaging, and energy squandering is kept to a minimum.
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