ppt Flashcards
Characteristics of living organisms:
1.
2.
3.
4.
5.
6.
- Consist of one or more cells
- Contain genetic information
- Use genetic information to reproduce
- Can convert molecules from their environment into new molecules
- Can extract energy from the environment to do biological work
- Regulate their internal environment
Cell Theory
- Basic structural and physiological unit of all life
- Cells come from cells
- Cell similar in chemical composition
- Most of chemical reactions of life occur within cells
- Sets of genetic information are replicated and passed on during cell division.
Eukaryotic cells evolved from
prokaryotes (endosymbiosis theory).
They have organelles.
Organelles—____ with specialized functions:
* nucleus
* chloroplast
* mitochondria
Membrane bound compartments
DNA: the information that is passed from __ to __cells.
Built of ____
Gene:
Mutations are ___ in the ____.
parent
daughter
repeating subunits–nucleotides
specific segment of DNA molecule, containing information for making proteins
alterations in the nucleotide sequence
Genome:
All cells in a multicellular organism
have ____.
all the nuclear DNA in the cell
the same genome
Living organisms interact:
– Individuals are part of ___.
Interacting populations of many different species form a ___.
Interacting communities in a given area form ___.
populations
community
ecosystems
Molecules in living organisms:
Most are ____.
proteins;
carbohydrates;
lipids;
nucleic acids
polymers formed by covalent
bonding of monomers
Polymers are formed by ___.
- Protein monomers =
- Carbohydrate monomers =
- Nucleic acid monomers =
- Lipids aren’t built of monomers but form ____.
covalent linkages of smaller units called monomers
amino acids
monosaccharides
nucleotides
large complexes considered as macromolecules
Reactions of Carbon compounds depend upon the presence of ___, each of which has ____ and ___ which it _____.
functional groups
specific chemical property
behavior
confers to the larger molecules
Six main functional groups:
__ = Hydroxyl – alcohols
__ = Carbonyl – aldehydes & ketones
__ = Carboxyl – acids
__ = amino – bases
__ = Phosphate - energy storage & transfer
__ = Sulfhydryl - cross links – similar to OH
-OH
-C=O
-COOH
-NH2
-PO4
-SH
Six main functional groups:
-OH =
-C=O =
-COOH =
-NH2 = amino – bases
-PO4 = Phosphate - energy storage & transfer
-SH = Sulfhydryl - cross links – similar to OH
Hydroxyl – alcohols
Carbonyl – aldehydes & ketones
Carboxyl – acids
Most biologic polymers are formed in ____. During which, _____.
These reactions require the following input:
condensation (dehydration synthesis) reactions
water molecule is removed
energy
Proteins have diverse structures & functions:
Proteins have important roles:
*
*
*
* Transport molecules
* Receptors
* Genetic regulatory molecules
* Structural units
enzymes
defensive molecules
hormonal/regulatory molecules
Proteins have diverse structures & functions:
Proteins have important roles:
* Enzymes
* Defensive molecules
* Hormonal/regulatory molecules
*
*
*
*
transport molecules
receptors
genetic regulatory molecules
structural units
Proteins made from ___.
- Proteins range in size from a few amino acids to thousands.
- Some proteins are composed of a single chain of amino acids, called a polypeptide. Other proteins
have more than one polypeptide chain. - ___ is crucial to the function of a protein and is influenced largely by the sequence of amino
acids. - Each different type of protein has a characteristic ___ composition and __.
20 different amino acid monomers
polypeptide
polypetide chain.
Folding
amino sequence acids
amino acid
order
Amino acid: protein’s building blocks
Due to the presence of the __and ___ group, amino acids are simultaneously acids and bases.
- The amino group is the basic __
part (__). The acid is a __group (__). - Differences in amino acids come from the __, attached to the
___ as the amino and the carboxyl
group
amino
carboxyl
nitrogen containing
(H2N)
carboxyl
(COOH)
side chains (R-groups)
same carbon
The α carbon is __because it is
bound to __ or __.
* Therefore, amino acids exist in two ___, __-amino acids and __- amino acids.
* Only __-amino acids commonly found in organisms.
asymmetrical
four different atoms
groups of atoms
isomeric forms
D
L
L
Amino acids can be classified based on the characteristics of their ___.
R-groups
- Charged hydrophilic side chains.
- Polar but uncharged side chains.
- Nonpolar hydrophobic side chains
__ amino acids attract ions of opposite charges.
___amino acids with __ but
___ form hydrogen bonds
Hydrophobic amino acids; nonpolar hydrophic chains
hydrophilic
hydrophobic
polar
uncharged side chains
Hydrophylic amino acids attract ___.
Hydrophylic amino acids with polar but uncharged side chains form ___
Hydrophobic amino acids; nonpolar hydrophic chains
ions of opposite charges
hydrogen bonds
Amino acids with special properties
* __ has a terminal —SH group, which allows it to form disulfide bridges with other __ molecules.
- __ has a hydrogen atom as the side chain. This makes it small enough to fit into small spaces and tight corners when the protein folds.
- __ has a modified amino group that forms a covalent bond with the R group. The ring limits rotation of the carbon’s bond.
__ is often found at bends and loops of proteins.
Cysteine
Glycine
Proline
Proteins are also called ___.
The first amino acid of a peptide is the ___ amino acid because the amino group is __ or __. The last amino acid of a peptide is the __ & has a __ group.
polypetides
N-terminus
free or unbound
C-terminus
free carboxyl
Amino acids with special properties
* Cysteine has a terminal —SH group, allowing it to form disulfide bridges with other cysteine molecules.
* Glycine has a hydrogen atom as the side chain. This makes it small enough to fit into small spaces and tight corners when the protein folds.
* Proline has a modified amino group that forms a covalent bond with the R group. The ring limits __ of the carbon’s bond.
Proline is often found at bends and loops of proteins.
folds
rotation
Primary Structure
Primary structure: the ___.
* It is determined by ___.
* It determines how, & where __ & __of the molecule may occur.
precise sequence of amino acids
covalent bonds
folding
bending
A protein’s secondary structure consists of the __, __ patterns in different __ of the ___chain.
- This shape is influenced primarily by __ arising from ___.
- The two common secondary structures, are the ___ & ___.
regular
repeated
regions
polypetide
hydrogen bonds
primary structure
α helix
β pleated sheet
Tertiary structure is the __
shape of the __, determined by
interactions among the __ of the amino acids.
- The outer surface of the protein
presents functional groups, which can interact with other molecules in the cell, such as other proteins or small molecules.
3-D shape
completed polypetide
side chains
Quaternary structure results from
___ ___ing and __ing.
multiple polypetide SUBUNITS
binding
interacting
Changes in __, __or high concentrations of __can change the __ of proteins. This loss of structure is called __.
temperature
PH
polar substances
3-D shape
structure
denaturation
____ is the 3-D shape of the completed polypeptide, determined by interactions among the side chains of the amino acids.
- The outer surface of the protein
presents ___, which can interact with other __ in the cell, such as
other proteins or small molecules.
Tertiary structure
functional groups
molecules
Six main functional groups:
