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Unit

Levels of Organization
Fundamentals of Anatomy & Physiology
Frederic H. Martini

PowerPoint Lecture Slides prepared by

Professor Albia Dugger, MiamiDade College, Miami, FL Professor Robert R. Speed, Ph.D., Wallace Community College, Dothan, AL
Copyright 2005 Pearson Education, Inc., publishing as Benjamin Cummings

Chapter 2: The Chemical Level of Organization

KEY CONCEPT
Matter is made up of atoms Atoms join together to form chemicals with different characteristics Chemical characteristics determine physiology at the molecular and cellular level

Atoms
Atoms are the smallest units of matter with their own chemical characteristics.
Atoms are divided into 2 basic regions: the central nucleus, contains heavy particles the electron cloud, contains very light, moving particles

Atomic Particles
Proton:
positive, 1 mass unit

Neutron:
neutral, 1 mass unit

Electron:
negative, low mass

Particles and Mass


Atomic number:
number of protons

Mass number:
number of protons plus neutrons

Atomic weight:
exact mass of all particles (daltons)

Isotopes
2 or more elements with equal numbers of protons but different numbers of neutrons

Elements
Are determined by the atomic number of an atom: are the most basic chemicals The atomic number is the number of protons The number of electrons in an element equals the number of protons

Elements in the Human Body

Table 21

Chemical Bonds
Ionic bonds:
attraction between cations and anions

Covalent bonds:
strong electron bonds

Hydrogen bonds:
weak polar bonds

Molecules and Compounds


Molecules:
atoms joined by strong bonds

Compounds:
atoms joined by strong or weak bonds

Ionic Bonds
(1) Ionic bonds form between atoms with opposite electrical charges (ions). An atom that loses electrons (electron donor) has a net positive charge, and is called a cation. An atom that gains electrons (electron acceptor) has a net negative charge, and is an anion

Figure 23a

Ionic Bonds
Are attractions between atoms with positive or negative charge

Figure 23b

Covalent Bonds
Covalent bonds occur when atoms share, rather than gain or lose electrons, forming molecules

Hydrogen Bonds
(3) Hydrogen bonds are weak attractions between the positive, hydrogen side of one polar molecule and the negative side of another polar molecule. Hydrogen bonds influence the shape of larger molecules, which is important to molecules such as proteins and DNA

Hydrogen bonds between H2O molecules cause surface tension

Figure 26

States of Matter
Solid:
constant volume and shape

Liquid:
constant volume but change shape

Gas:
change volume and shape

Why are chemical reactions important to physiology?

Energy
Energy:
the power to do work

Work:
a change in mass or distance

Forms of Energy
Kinetic energy:
energy of motion

Potential energy:
stored energy

Chemical energy:
potential energy stored in chemical bonds

KEY CONCEPT
When energy is exchanged, heat is produced, but cells cannot capture it or use it for work

Break Down, Build Up


Decomposition reaction (catabolism):
AB A + B

Synthesis reaction (anabolism):


A + B AB

Exchange reaction (reversible):


AB + C AC + B AB + CD AC + BD

Water In, Water Out


Hydrolysis:
ABCDE + H2O ABCH + HODE

Dehydration synthesis (condensation):


ABCH + HODE ABCDE + H2O

KEY CONCEPT
Reversible reactions seek equilibrium, balancing opposing reaction rates
Add or remove reactants:
reaction rates adjust to reach a new equilibrium

Materials in Reactions
Reactants:
materials going into a reaction

Products:
materials coming out of a reaction

Enzymes:
proteins that lower the activation energy of a reaction

Activation Energy
Chemical reactions in cells cannot start without help Activation energy gets a reaction started

Figure 27

Enzymes

Enzymes are proteins that act as catalysts they are just facilitators speeding up the chemical reaction One specific enzyme reduces the activation energy for one specific reaction. Enzymes are not used up in a reaction

Energy In, Energy Out


Exergonic reactions: A chemical reaction which releases more energy than it uses to get started is an exergonic reaction (exo = outside). Endergonic reactions: When the activation energy of a reaction is greater than the energy it produces, it is an endergonic reaction (endo = inside).

Endergonic reactions: use more energy than they produce Exergonic reactions: produce more energy than they use

KEY CONCEPT
Most chemical reactions that sustain life cannot occur unless the right enzymes are present

Organic and Inorganic Molecules


Organic:
molecules based on carbon and hydrogen

Inorganic:
molecules not based on carbon and hydrogen

Essential Molecules
Nutrients:
essential molecules obtained from food

Metabolites:
molecules made or broken down in the body

Why is water so important to life? Properties of Water (1 of 2)


Solubility:
waters ability to dissolve a solute in a solvent to make a solution

Reactivity:
most body chemistry uses or occurs in water

Properties of Water (2 of 2)
High heat capacity:
waters ability to absorb and retain heat

Lubrication:
to moisten and reduce friction

KEY CONCEPT
Most of our body weight is water Water is the key structural and functional component of cells and their control mechanisms, the nucleic acids

Aqueous Solutions
Polar water molecules form hydration spheres around ions and small polar molecules to keep them in solution

Figure 28

Electrolytes
Inorganic ions which conduct electricity in solution Electrolyte imbalance seriously disturbs vital body functions

Molecules and Water


Hydrophilic:
hydro = water, philos = loving reacts with water

Hydrophobic:
phobos = fear does not react with water

Solutions
Colloid:
a solution of very large organic molecules

Suspension:
a solution in which particles settle (sediment)

Concentration:
the amount of solute in a solvent (mol/L, mg/mL)

pH
pH:
the concentration of hydrogen ions (H+) in a solution

Neutral pH:
a balance of H+ and OH pure water = 7.0

Acids and Bases


Acid (acidic): pH lower than 7.0 high H+ concentration, low OH concentration Base (basic): pH higher than 7.0 low H+ concentration, high OH concentration

pH Scale
Has an inverse relationship with H+ concentration: more H+ ions mean lower pH, less H+ ions mean higher pH

Figure 29

KEY CONCEPT
pH of body fluids measures free H+ ions in solution Excess H+ ions (low pH):
damages cells and tissues alters proteins interferes with normal physiological functions

Excess OH ions (high pH) also cause problems, but rarely

Acid and Alkaline


Acidosis:
excess H+ in body fluid (low pH)

Alkalosis:
excess OH in body fluid (high pH)

Controlling pH
Salts:
positive or negative ions in solution contain no H+ or OH (NaCl)

Buffers:
weak acid/salt compounds neutralizes either strong acid or strong base

What kinds of organic compounds are there, and how do they work?

Functional Groups
Molecular groups which allow molecules to interact with other molecules

Table 24

Simple Sugars
Monosaccharides:
simple sugars with 3 to 7 carbon atoms (glucose)

Disaccharides:
2 simple sugars condensed by dehydration synthesis (sucrose)

Polysaccharides
Chains of many simple sugars (glycogen)

Figure 212

Carbohydrate Functions

Table 25

KEY CONCEPT
Carbohydrates are quick energy sources and components of membranes Lipids have many functions, including membrane structure and energy storage

Lipids
Mainly hydrophobic molecules such as fats, oils, and waxes Made mostly of carbon and hydrogen atoms

PLAY

Lipids

Classes of Lipids
Fatty acids Eicosanoids Glycerides Steroids Phospholipids and glycolipids

Saturated and Unsaturated


Fatty acids may be:
saturated with hydrogen (no covalent bonds) unsaturated (1 or more double bonds)

Types of Eicosanoids
Leukotrienes:
active in immune system

Prostaglandins:
local hormones, short-chain fatty acids

Glycerides
Glycerides: are the fatty acids attached to a glycerol molecule Triglyceride: are the 3 fatty-acid tails, fat storage molecule
Figure 215

Steroids
4 carbon rings

Figure 216

Types of Steroids
Cholesterol:
component of cell membranes

Estrogens and testosterone:


sex hormones

Corticosteroids and calcitrol:


metabolic regulation

Bile salts:
derived from steroids

Combination Lipids

Figure 217a, b

Phospholipids and Glycolipids


Have hydrophilic heads and hydrophobic tails Are structural lipids, components of cell membranes

5 Lipid Types

Table 26

Protein Structure
Proteins are the most abundant and important organic molecules Basic elements:
carbon (C), hydrogen (H), oxygen (O), and nitrogen (N)

Basic building blocks:


20 amino acids
Proteins

PLAY

Protein Functions
7 major protein functions:
1. support: structural proteins 2. movement: contractile proteins 3. transport: transport proteins 4. buffering: regulation of pH 5. metabolic regulation: enzymes 6. coordination and control: hormones 7. defense: antibodies

KEY CONCEPT
Proteins:
control anatomical structure and physiological function determine cell shape and tissue properties perform almost all cell functions

Amino Acid Structure


1. central carbon 2. hydrogen 3. amino group ( NH2) 4. carboxylic acid group (COOH) 5. variable side chain or R group

Peptide Bond
A dehydration synthesis between:
the amino group of 1 amino acid and the carboxylic acid group of another amino acid producing a peptide

Protein structure
For the polypeptide chain to become a protein, it must be folded into a unique shape. Proteins have 4 levels of shape: (1) primary structure: the order of amino acids (2) secondary structure: hydrogen bonds form (3) tertiary structure: folds the secondary structure (4) quaternary structure: several tertiary structures together

Primary Structure
Polypeptide:
a long chain of amino acids

Figure 220a

Secondary Structure
Hydrogen bonds form spirals or pleats

Figure 220b

Tertiary Structure
Secondary structure folds into a unique shape

Figure 220c

Quaternary Structure
Final protein shape:
several tertiary structures together

Figure 220d

Shape and Function


Protein function is based on shape Shape is based on sequence of amino acids Denaturation:
loss of shape and function due to heat or pH

Protein Shapes
Fibrous proteins:
structural sheets or strands

Globular proteins:
soluble spheres with active functions

Enzymes
Enzymes are catalysts:
proteins that lower the activation energy of a chemical reaction are not changed or used up in the reaction

PLAY

Enzymes

How Enzymes Work

Figure 221

How Enzymes Work


Substrates:
reactants in enzymatic reactions

Active site:
a location on an enzyme that fits a particular substrate

Enzyme Helpers
Cofactor:
an ion or molecule that binds to an enzyme before substrates can bind

Coenzyme:
nonprotein organic cofactors (vitamins)

Isozymes:
2 enzymes that can catalyze the same reaction

Enzyme Characteristics
Specificity:
one enzyme catalyzes one reaction

Saturation limits:
an enzymes maximum work rate

Regulation:
the ability to turn off and on

Protein Combinations
Glycoproteins:
large protein + small carbohydrate
includes enzymes, antibodies, hormones, and mucus production

Proteoglycans:
large polysaccharides + polypeptides
promote viscosity

Nucleic Acids
Large organic molecules, found in the nucleus, which store and process information at the molecular level DNA and RNA

Deoxyribonucleic Acid (DNA)


Determines inherited characteristics Directs protein synthesis Controls enzyme production Controls metabolism

Ribonucleic Acid (RNA)


Codes intermediate steps in protein synthesis

KEY CONCEPT
DNA in the cell nucleus contains the information needed to construct all of the proteins in the body

Nucleotides
Are the building blocks of DNA Have 3 molecular parts:
sugar (deoxyribose) phosphate group nitrogenous base (A, G, T, C)

PLAY

Nucleotides

The Bases

Figure 222b, c

Complementary Bases
Complementary base pairs:
purines pair with pyrimidines:
DNA:
adenine (A) and thymine (T) cytosine (C) and guanine (G)

RNA:
uracil (U) replaces thymine (T)

Nucleic Acids
Long chains of nucleotides form RNA and DNA

Figure 223

RNA and DNA

Table 28

RNA and DNA


RNA:
a single strand

DNA:
a double helix joined at bases by hydrogen bonds

Forms of RNA
messenger RNA (mRNA) transfer RNA (tRNA) ribosomal RNA (rRNA)

ADP and ATP


adenosine diphosphate (ADP):
2 phosphate groups
di = 2

adenosine triphosphate (ATP):


3 phosphate groups
tri = 3

Phosphorylation
Adding a phosphate group to ADP with a high-energy bond to form the highenergy compound ATP ATPase:
the enzyme that catalyzes phophorylation

The Energy Molecule


Chemical energy stored in phosphate bonds

Figure 224

Compounds Important to Physiology

Table 28

Recycling Old Molecules

Table 29

KEY CONCEPT
Your body recycles and renews all of its chemical components at intervals ranging from minutes to years Metabolic turnover lets your body grow, change and adapt to new conditions and activities

SUMMARY (1 of 2)
Atoms, molecules, and chemical bonds control cellular physiology Metabolism and energy work within the cell Importance of organic and inorganic nutrients and metabolites

SUMMARY (2 of 2)
Role of water and solubility in metabolism and cell structure Chemistry of acids and bases, pH and buffers Structure and function of carbohydrates, lipids, proteins, and nucleic acids