chapter 1 Flashcards
3 levels of organization
cellular level, organismal level, populational level
atoms
smallest unit of an element
elements
substances that cant be degraded into a different substance
compounds
composed of 2 or more elements in unvarying proportions
Example: H2O
Biomolecule
Molecules of life
Proteins, carbohydrates, lipids, nucleic acid
organelles
membrane bound SACS with specialized functions
cells
smallest living unit
The 2 types of cells
Prokaryote & Eukaryote
Prokaryote
“simple Cells” DONT have compartmentalized organelles
Example- bacteria
Eukaryote
“complex cells” WILL have compartmentalized organelles
example- skin cell
Tissues
composed of a group of cells performing a specialized function
Organs
Composed of tissue in a specific pattern to cause a specific function
systems
composed of 2 or more organs that are interacting
characteristics of living things
have organization, need energy, respond to a stimulus, adaptation, want homeostasis, reproduction, mitosis, meiosis, develop & grow, locomotion
anabolism
“synthesis” combining small molecules to make large molecules
catabolism
“degradation” breaking down large molecules into smaller molecules and creating energy
Mitosis
reproduction of somatic (non-sex cells) cells
cells are genetically identical
meiosis
reproduction of sex cells (sperm & egg)
cells are NOT genetically identical
locomotion
ability to move cellular locomotion
cilia
hair like projections on cells
flagellum
whip like structure found on sperm
pseudopodia
“false feet”
atomic number
total number of protons an element has. tells number of electrons
mass number/atomic weight
weight of all protons & weight of all neutrons
weight of nucleus
isotopes
different forms of SAME element. same number of electrons & protons BUT different number of neutrons
columns
elements in same column have same number of electrons that can participate in forming a bond
rows
elements in the same row have same number of energy shells or orbitals
4 types of sub orbitals
S=2 electrons
P=6 electrons
D=10 electrons
F=14 electrons
electronic configuration
language used to identify an element & to identify placement of electrons
Types of elements
noble gases, non-metals, metalloids & metals
noble gases
DONT participate in bond formation
non-metals
dull appearance & poor conductors of electricity, they accept electrons
metalloids
have metal & non-metal characteristics
metals
shiny, good conductors of electricity, donate electrons
chemical bonds
a union between the electrons of 2+ elements
ionic bonds
formed between a metal & non metal. complete transfer of electrons from a metal to a non metal. bonds are easily broken
two types of ions
anion & cation
anion
negative charged, accept electrons
cation
positively charged, donate electrons
covalent bonds
formed between 2+ nonmetals. theres a sharing of electrons. require a large amount of energy to be broken
EX. H2O
Water is a…
polar molecule (hydrophilic-water loving)
Acids & bases
measured by the amount of H+ & OH- ions
uses pH scales as the method of measurement
pH scale
0 acidic
7 neutral
8 basic
buffering systems
a system which prevents large changes in pH
Molecules of life
proteins, lipids, carbohydrates, nucleic acids
two classes of molecules
inorganic & organic
inorganic
do not contain carbon in their backbone structure
organic
molecules that contain carbon in their backbone structure
Ex. proteins, carbohydrates, lipids & nucleic acids
different types of organic molecules
they each have their own functional group
functional groups cluster of atoms that impart distinct properties to a molecule
polymers
large molecules like proteins, lipids, nucleic acids & carbohydrates
they are composed of monomers
monomers
smaller components of polymers
carbohydrates
can be a polymer (composed of sugar units)
or a monomer (composed of a single sugar unit)
most abundant biological molecules - hydrophilic
functions of carbohydrates
primary source of energy
participate in cell- cell recognition
responsible for the different blood types
different classes of carbohydrates
monosaccharides
disaccharides
monosaccharides
composed of a single sugar unit
EX glucose, fructose & galactose
disaccharides
composed of 2 sugar units held together by a glycosidic bond
EX sucrose, maltose, lactose
oligosaccharide
composed of 3-200 sugar units
polysaccharides
composed of many (hundreds-thousands) sugar units
EX starch & glycogen. Composed of glucose molecules
lipids
known as fats & triacylglycerides
greasy or oily compounds that are hydroPHOBIC
secondary source of energy
functions of lipids
provide insulation, maintain body temp, protect organs, precursors for sex hormones, components of the cells plasma membrane
structure of lipids
composed of a glycerol molecule with fatty acids tails (monomer)
classes of lipids
saturated & unsaturated
saturated lipids
DONT contain double bonds in their fatty acid chains. they are solid at room temp
unsaturated lipids
DO contain double bonds in their fatty acid chains, they are liquid at room temp
nucleic acids
composed of monomers of nucleotides (composed of sugar, phosphate group & nitrogen bases)
two types of nucleic acids
DNA & RNA
function of nucleic acids
serve as blue print for proteins
composition of nucleotides
DNA & RNA
nitrogen bases - Purine (adenine & granine) Pyrimidines (thymine, cytosine & uracil)
- phosphate group
DNA
sugar deoxyribose, bases (A=T) (C=G), location is nucleus & mitochondria structure is double stranded
RNA
ribose, A=U C=G, found in ribosomes, nucleus, cytoplasm. structure is single stranded
composition of proteins
monomers & amino acids
monomers
proteins are composed of amino acids
amino acids
chemical molecules that are composed of an amino group & a carboxyl group. held together by a peptide bond
R chain
helps identify the amino acid & gives its function
4 shapes of proteins
primary, secondary, teritary & quaternary
primary structure
amino acid sequence of the protein. its linear arrangement of the aminos acids which are held together by peptide bonds
secondary structure
represents the coiling or folding of the primary structure. held together by hydrogen bonds
teritary structure
represents the folding of the secondary structures. also held together by hydrogen bonds
quarternary structure
the final folding of the protein structure. it is held together by hydrogen bonds. these structures form subunits within the protein (100% active)
When non-covalent bonds are broken…
this disrupts the proteins 3D shape. AKA denaturation. it can be caused by changes in pH, temp & ionic concentration