The main components in organic molecules (replace H attached to carbon skeletons)number and shape give each molecule its unique property
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All Functional groups
Hydroxyl (OH) - alcohol
Carbonyl (C=O)- Ketones and Aldehydes
Carboxyl( OH-C=O) - Carboxylic acid
Amino Group(H-N-H)- Amine
Phosphate PO4 - Organic phosphate
Sulfhydral -SH -thiol
Methyl CH3- Methylated Compund
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Ester Linkage
In fats (O-C=O) Attaches Glycerol (CH2O) and Fatty Acids
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Ketones
When Carbonyl group is in the C skeleton
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Aldehyde
Wehn Carbonyl group is on the end of the skeleton
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What is ATP
Adenosine Triphosphate - Has potential to react with water releasing energy
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ADP
formed when ATP reacts with water and releases a Phosphate as a Pi and becomes Adenosine diphosphate
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Monomers
Repeating units and builiding blocks of polymers
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Polymers
made up of monomers include: Carbohydrates, proteins, and nucleic acids
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What do enzymes do
Speed up Chemical Reactions or Break down polymers
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Dehydration Reaction
forms or synthesizes a polymer. combines. molecules with the loss of water (H2O)
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Hydrolysis Reaction
Breaks down polymer with the use of water
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Carbohydrates
Are polymers of sugars
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Monosachirrides
Simple sugars like glucose
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Polysacharrides
Complex sugars polymer of many sugars with storage (starch and structural (cell wall) roles
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What are Lipids
Hydrophobic Fats Phospholipids and Steroids consisting mostly of hydrocarbon
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Saturated Fatty acids
maximum number of hydrogen atoms possible and no double bonds (solid)
Bad for you lead to heart problems
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Unsaturated Fatty Acids
one or more double bonds whihc cause bending (liquid)
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Trans Fats
Worst for health reduce HDL and increase LDL
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Phospholipids
Form membrane bilayer with hydrophilic heads and hydrophobic tails. Made of a phosphate attached to a glycerol with two fatty acid tails O<
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Steroids
Type of lipids made of a carbon skeleton with 4 fused rings
\
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Protein
diversity of structures, resulting in a wide range of functions. make up most dry mass in cells. Very complex. Consist of Amino group R-group and Carboxyl Group
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Protein Functions
Enzymes (break down/speed up), defense, storage, transport, cellular \n communication, movement, and structural support
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Catabolic
Break down of molecules
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Anabolic
Creating bigger molecules
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Enzymatic proteins
Catalysts that speed up chemical process
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Defense Proteins
Defend against disease (antibodies)
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Storage proteins
Store amino acids
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Transport proteins
transport substances ex. hemoglobin transports oxygen
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Hormonal Proteins
Coordinate organisms activities like insulin controlling high blood sugar
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Receptor Proteins
Recieve signals of chemica stimuli
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Contractile and Motor Proteins
Movement like cilia and flagella as well as muscles
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Structural proteins
support like keratin
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Monomer of protein
Amino acid
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Side chains of Amino acids
Hydrophobic and hydrophilic side chains
Electrically charged side chains are hydrophilic +-acidic. -is basic
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Polypeptides
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Amino Acids
monomer of Protein and Polypeptide linked by covalent bonds called peptide bonds
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Four levels of protein structure
\n โ Primary structure is determined by inherited genetic \n information The primary structure of a protein is the unique \n sequence of amino acids \n โข Secondary structure consists of coils and folds in the \n polypeptide chain \n โข Tertiary structure is determined by interactions \n among various side chains (R groups) \n โข Quaternary structure results when a protein consists \n of multiple polypeptide chains
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Nucleic acids
store transmit and help express hereditary info (DNA) (RNA) polymer of nucleotide
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Nucleotide
Consist of Nitrogenous Base, one or more Phosphate groups and Pentose (5 Carbon sugar)
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Nucleoside
Nucleotide minus the Phosphate
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Pyrimidines
\[cytosine (C), thymine (T), and uracil (U)\] have a single six-membered ring
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Purines
\[adenine (A) and guanine (G)\] have a six-membered ring fused to a five-membered \n ring
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Basic features of all cells
Plasma membrane-
Cytosol or Cytoplasm - semifluid substance bound to membrane
Chromosomes- Carry genes
Ribosomes- make proteins
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All places DNA is located
Nucleus Mitochondria and Cytoplasm
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Chromatin
DNA and protein of chromosomes condenses to form discrete chromosomes as a cell prepares to divide
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Where is Ribosomal rRna synthesized
nucleoulus
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Ribosomes
are complexes made of ribosomal \n RNA and protein
* Carry out protein synthesis * In the cytosol =(free ribosomes) \n Ribosomes on endoplasmic reticulum or the nuclear \n envelope =(bound ribosomes)
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Endoplasmic Reticulum
The endoplasmic reticulum (ER) accounts for more than half of the total membrane \n in many eukaryotic cells ER membrane is continuous with the nuclear \n envelope
Two distinct regions of ER: \n - Smooth ER (lacks ribosomes)
\- Rough ER (surface has ribosomes)
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Smooth ER functions
* No ribosomes attach to it * Synthesizes lipids * Metabolizes carbohydrates * Detoxifies drugs and poisons * Stores calcium ions
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Rough ER functions
* ER is bound ribosomes, which secrete glycoproteins (proteins covalently bonded to carbohydrates) * Distributes transport vesicles (secretory proteins surrounded by membranes) * a membrane factory for the cell
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Golgi Apparatus
Consist of Flattened membranous sacs called cisternae
* Modifies products of the ER * Manufactures certain macromolecules * Sorts and packages materials into transport vesicles
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Lysosome
membranous sac of hydrolytic enzymes which digest macromolecules
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Phagocytosis
Cell engulfing another cell
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Autophagy
\n recycle the cellโs own organelles and macromolecules,
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Vacuoles
large vesicles derived from the ER and Golgi apparatus
* Vacuoles perform a variety of functions in different kinds \n of cells
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Food Vacuoles
created through phagocytosis (Vacuole with a digestive function)
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Contractile Vacuoles
Pump out excess water
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Central Vacuoles
hold organic compounds and water
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Peripheral Proteins
Bound to surface of membrane
* Transport * Enzymatic activity * Signal transduction * Cell-cell recognition * Intercellular joining * Attachment to the cytoskeleton and extracellular matrix \n (ECM)