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Fundamentals of Anatomy & Physiology
Frederic H. Martini
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
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
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
Table 21
Chemical Bonds
Ionic bonds:
attraction between cations and anions
Covalent bonds:
strong electron bonds
Hydrogen bonds:
weak polar 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
Figure 26
States of Matter
Solid:
constant volume and shape
Liquid:
constant volume but change shape
Gas:
change volume and shape
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
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
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
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
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
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
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
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
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
Bile salts:
derived from steroids
Combination Lipids
Figure 217a, b
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)
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
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
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
Figure 221
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
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
Table 28
DNA:
a double helix joined at bases by hydrogen bonds
Forms of RNA
messenger RNA (mRNA) transfer RNA (tRNA) ribosomal RNA (rRNA)
Phosphorylation
Adding a phosphate group to ADP with a high-energy bond to form the highenergy compound ATP ATPase:
the enzyme that catalyzes phophorylation
Figure 224
Table 28
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