Title: Basic Cell Chemistry
1Basic Cell Chemistry
2Chapter Goals
- After studying this chapter, students should be
able to - describe the structure of an atom and define the
terms atomic mass, atomic number, and ion. - explain how covalent bonds are formed and
distinguish between nonpolar and polar covalent
bonds. - describe the structure of an ion and explain how
ionic bonds are formed. - describe the nature of hydrogen bonds and explain
their significance. - describe the structure of a water molecule and
explain why some compounds are hydrophilic and
others are hydrophobic. - define the terms acid and base and explain the
meaning of the pH scale. - explain how the pH of the blood is stabilized by
bicarbonate buffer, and define the terms acidosis
and alkalosis. - describe the different types of carbohydrates and
give examples of each type.
3Chapter Goals (contd)
- After studying this chapter, students should be
able to - describe the mechanisms and significance of
dehydration synthesis and hydrolysis reactions
and explain their significance. - state the common characteristics of lipids and
describe the different categories of lipids. - describe how peptide bonds are formed and the
different orders of protein structure. - list some of the functions of proteins and
explain why proteins provide specificity in their
functions. - tell what enzymes are and how they work.
- understand the concept of optima
- understand basic enzyme kinetics
4Basic Cell Chemistry
- Matter and elements
- Atomic structure
- Ions
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7Atomic Structure
8Ionic Bond
Atomic 11 Atomic Mass 23
Atomic 17 Atomic Mass 34
9Crystalline Lattice
10Covalent Bond
11 12 13 14Polar Molecule
15Hydrogen Bond
16 17Acids, Bases and Salts
- Acid - proton donor
- pH -logH
- Scale 1 - 14, with 7 being neutral
- Base - proton acceptor
- Salts - crystalline solids produced by
neutralization reactions. - Buffers resist change in pH
18Biomolecules
- Functional Groups
- Carbohydrates
- Lipids
- Nucleic Acids
- Proteins
19 20 21Carbohydrates (CH2O)
- Monosaccharides
- Triose
- Tetrose
- Pentose
- Hexose
- Disaccharides
- Oligosaccharides
- Polysaccharides
22Hexose Monosaccharide (glucose)
23 24Polysaccharide (glycogen)
25Lipids
- Glycerides (Mono, Di, Tri)
- Phospholipids
- Steroids
- Prostaglandins
26Triglyceride
27Phospholipid and Sphingolipids
28Steroid
29Steroid Examples
30 31Proteins
- Basic building blocks (amino acids)
- Primary Structure
- Secondary Structure
- Tertiary Structure
- Quaternary Structure
32Amino Acid
B-13
33Peptide Bond
B-14
34Primary Structure
B-15
35Levels of Structure
B-16
36Side Chain Interactions
B-17
37Nucleic Acids
- Building Blocks (Nucleotides)
- DNA
- RNA
38Structure of Nucleotide Triphosphate
B-18
39Enzymes
- Specific organic catalysts
- Cannot drive reactions
- Direction determined by LeChatlier Principle.
- E S lt--gt ES lt--gt E P
- E enzyme S substrate P product
404.1a
414.1b
424.2
43Induced Fit Model
Binding of substrate causes the enzyme to change
shape such that the enzyme fits around the
substrate.
444.3
454.4
464.5
474.6
484.8
494.9
504.10
51Chapter Summary
- Atoms, Ions, and Chemical Bonds
- Carbohydrates and Lipids
- Proteins
52Atoms, Ions, and Chemical Bonds
- I. Covalent bonds are formed by atoms that share
electrons. They are the strongest type of
chemical bond. - A. Electrons are equally shared in nonpolar
covalent bonds and unequally shared in polar
covalent bonds. - B. Atoms of oxygen, nitrogen, and phosphorus
strongly attract electrons and become
electrically negative compared to the other atoms
sharing electrons with them.
53Atoms, Ions, and Chemical Bonds
- II. Ionic bonds are formed by atoms that transfer
electrons these weak bonds join atoms together
in an ionic compound. - A. If one atom in this compound takes the
electron from another atom, it gains a net
negative charge and the other atom becomes
positively charged. - B. Ionic bonds easily break when the ionic
compound is dissolved in water. Dissociation of
the ionic compound yields charged atoms called
ions.
54Atoms, Ions, and Chemical Bonds
- III. When hydrogen is bonded to an
electronegative atom, it gains a slight positive
charge and is weakly attracted to another
electronegative atom. This weak attraction is a
hydrogen bond.
55Atoms, Ions, and Chemical Bonds
- IV. Acids donate hydrogen ions to solution,
whereas bases lower the hydrogen ion
concentration on a solution. - A. The pH scale is a negative function of the
logarithm of the hydrogen ion concentration. - B. In a neutral solution the concentration of H
is equal to the concentration of OH-, and the pH
is 7. - C. Acids raise the H concentration and thus
lower the pH below 7 bases lower the H
concentration and thus raise the pH above 7.
56Atoms, Ions, and Chemical Bonds
- V. Organic molecules contain atoms of carbon
joined together by covalent bonds atoms of
nitrogen, oxygen, phosphorus, or sulfur may be
present as specific functional groups in the
organic molecule.
57Carbohydrates and Lipids
- I. Carbohydrates contain carbon, hydrogen, and
oxygen, usually in a ratio of 121. - A. Carbohydrates consist of simple sugars
(monosaccharides), disaccharides, and
polysaccharides (such as glycogen). - B. Covalent bonds between monosaccharides are
formed by dehydration synthesis, or condensation.
Bonds are broken by hydrolysis reactions.
58Carbohydrates and Lipids
- II. Lipids are organic molecules that are
insoluble in polar solvents such as water. - A. Triglycerides (fat and oil) consist of three
fatty acid molecules joined to a molecule of
glycerol. - B. Ketone bodies are smaller derivations of fatty
acids. - C. Phospholipids (such as lecithin) are
phosphate-containing lipids that have a
hydrophilic polar group. The rest of the molecule
is hydrophobic. - D. Steroids (including the hormones of the
adrenal cortex and gonads) are lipids with a
characteristic five-ring structure. - E. Prostaglandins are a family of cyclic fatty
acids, which serve a variety of regulatory
functions
59Proteins
- I. Proteins are composed of long chains of amino
acids bound together by covalent peptide bonds. - A. Each amino acid contains an amino group, a
carboxyl group, and a functional group.
Differences in the functional groups give each of
the more than twenty different amino acids an
individual identity. - B. The polypeptide chain may be twisted into a
helix (secondary structure) and bent and folded
to form the tertiary structure of the protein. - C. Proteins that are composed of two or more
polypeptide chains are said to have a quaternary
structure. - D. Proteins may be combined with carbohydrates,
lipids, or other molecules. - E. Because of their great variety of possible
structures, proteins serve a wider variety of
specific functions than any other type of
molecule.
60Enzymes
- I. Enzymes are specific organic catalysts
- A. Most enzymes are proteins.
- B. Enzymes have a unique 3-D structure that
enables them to bind to a specific substrate. - C. Enzymes speed up chemical reactions by
lowering activation energy. - D. Since enzymes physically join to their
substrate, they can become saturated. - E. The structure of enzymes is encoded in DNA, so
a mutation can affect enzyme structure.