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Biological important chemical groups?
alcohol, aldehyde, ketone, carboxylic acid, amine, sulfhydryl, organic phosphate
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Methyl Group?
CH3, not reactive, acts as recognizable tag on biological molecules
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Alcohol Hydroxyl
polar, can form H bonds with H2O to dissolve organic compounds (example: sugar)
R - OH
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Aldehyde Carbonyl
end of C skeleton, can be structural isomers with different properties, ex: acetone and propanol
C is double bonded to O, single bond w/ H
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Ketone Carbonyl
within the C skeleton, can be structural isomers with different properties, example: aldoses and ketoses
Carbon is double bonded with O
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Carboxyl Group
very polar, has acidic properties (source of H+ ions), WEAK ACID
cabon is double bonded to O, single bonded to OH
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Amino Group
acts as a base, can pick up H+ from surrounding solution, WEAK BASE
NH2 base
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Sulfhydryl Group
two can react to form covalent bond, allows crosslinking to stabilize protein structures (ie: maintains curliness of hair)
SH base
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Phosphate Group
phosphoric acid that loss 2 Hydrogens, partakes in many chemical reactions with H2O which leads to release of energy
Phosphate is double bonded to an O (top), single bonded to OH (right), single bonded to OH (bottom), and single bonded to O (left)
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Ester?
formed by combining alcohol and a carboxylic acid
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Amide?
formed by combining amine and carboxylic acid
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Phosphoester?
formed by combining alcohol and phosphoric acid
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Transesterification?
used in synthesis of polyester, combines alcohol and ester to form a different alcohol and different ester
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4 large biological molecules?
Carbohydrates, Lipids, Proteins, Nucleic acid
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Macromolecules?
composed of THOUSANDS of covalently connected atoms
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Polymer?
long molecule that consists of many monomers
Carbohydrates, proteins, and nucleic acids are considered polymers
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Monomers?
small building blocks of molecules that combine to create a polymer
Monosaccharide (sugar), nucleotide, amino acid
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Condensation/dehydration reaction?
two monomers bond together and lose a water molecule
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Enzymes?
macromolecules that speed up dehydration process, some are protein based, some are RNA based, acts as catalyst, NOT CONSUMED, perform functions repeatedly, functions as workhorses that carry out processes of life
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Hydrolysis?
reverse reaction of dehydration; dissembles polymers to monomers
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Simple Polymer?
oligosaccharide, oligonucleotide, peptide
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Complex Polymer?
polysaccharide, nucleic acid, polypeptide protein
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Proteins
accounts for more than 50% of dry mass of most cells, functions include: enzymatic functions, structural support, storage, transport, cellular communication, movement, and defense against foreign substances
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Enzymatic Proteins?
acceleration of chemical reactions
Digestive enzymes
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Structural proteins
support
silk fibers, collagen and elastin in animal connective tissues, etc.
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Storage proteins
storage of AMINO ACIDS
ovalbumin in egg white caseins, protein of milk, storage proteins in plant seeds
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Transport protein
transport of other substances
Hemoglobin
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Hormonal proteins
coordinates an organism's activities
Insulin, hormone secreted by pancreas
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Receptor proteins
response of cell to chemical stimuli
receptors in nerve cell membranes
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Contractile and motor proteins
movement
actin and myosin in muscles, proteins in cilia and flagella
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Defensive proteins
protection against disease
Antibodies combat bacteria and viruses
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Polypeptides
built from same set of 20 amino acids, consists of multiple peptides (proteins consist of 1 or more polypeptides)
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Nonpolar covalent bond?
atoms share the electron equally
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polar covalent bond?
one atoms is more EN, atoms are NOT shared equally (electrons)
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Polar amino acids
contain functional groups in side chains, can hydrogen bond with other groups, hydrophilic and often found on surface of proteins
- Polar uncharged: S, T, C, Y, N, Q
- Polar charged: D & E (acidic), K, R, H (basic)
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Protein primary structure
determined by unique sequence of amino acids and inherited genetic information, sequence in which monomers are connected
shows covalent peptide bonds
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Protein secondary structure
found in most proteins, consists of coils and folds in polypeptide chain, local ways of founding polymers
shows hydrogen bonds
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Protein tertiary structure
determined by interactions among various side chains (R groups), overal fold of molecule (3D or symmetrical)
hydrophobic interactions, Van Der Waals interactions, Ionic bonds, hydrogen bonds
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Protein quarternary structure
results when protein consists of multiple polypeptide chains, intermolecular associations
hydrophobic interactions, Van Der Waals interactions, Ionic bonds, hydrogen bonds
Collagen (fibrous protein and most abundant protein in mammals) and Hemoglobin (4 polypeptides)
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Cofactors?
Myoglobin stores O2, Hemoglobin transports O2, both use Heme cofactors to bind O2; some proteins bind ions and/or organic molecules to help fulfill their function
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What determines a protein structure?
physical and chemical conditions can affect structure, alterations to pH, salt concentration, temperature, other environment factors
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Denaturation?
loss of protein's native structure; biologicall inactive, can be reverse
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Carbohydrates?
sugars, polymers of sugars
contains Carbon, hydrogen, and oxygen in ratio of CH2O
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Disaccharide?
dehydration reaction that joins two monosaccharides; forms covalent bond called glycosidic linkage
ex: Maltose, Sucrose, Lactose
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Polysaccharides?
polymers of sugar, storage and structure roles, hundreds to thousands of monosaccharides
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Starch
storage polysaccharides of plants, consists entirely of glucose monomers
unbranched = amylose, branched = amylopectin
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Glycogen?
storage polysaccharide in animals, more branched than amylopectin; humans store glycogen in liver and muscle cells
Diabetes is cause of glycogen metabolism
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Alpha glucose?
polymers that have a helical structure
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Beta glucose?
polymers that have a straight structure
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Nucleotides?
consists of 3 components: Nitrogenous base, sugar, and phosphate
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Lipids?
group of molecules that are water-insoluble (hydrophobic!!!), nonpolar covalent bonds, do not form polymers
Fats, oils, waxes, phospholipids, steroids, carotenoids
bold = biologically important lipids
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Fats
constructed from two smaller molecules by dehydration reaction (glycerol and fatty acids), forms triacylglycerol
glycerol = 3 carbon alcohol w/ hydroxyl group attack to each carbon
fatty acid = carboxyl group attached to long hydrocarbon skeleton
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wax?
type of lipid, natural secretions of plants and animals
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saturated fatty acids?
maximum # of hydrogen atoms possible, no double bonds, tight packing = solid @ RT
animal fats are usually saturated fat
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unsaturated fatty acids?
1 or more double bonds, kinks prevent tight packing, liquid @ RT
plant fats and fish fats are usually unsaturated
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Hydrogenation?
process of converting unsaturated fats to saturated fats by adding hydrogen, creates unsaturated fat with trans double bonds in addition to saturated ones
trans fat = very very bad
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Functions of fat?
energy storage (twice as much energy as same mass of polysaccharides such as starch)
humans store fat in adipose cells; adipose tissues also cushions vital organs and insulates body
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Phopholipids?
two fatty acids and a phosphate are attached to glycerol
hydrophilic head and hydrophobic tails
Major components of all cell membranes
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Steroids?
lipids characterized by carbon skeleton, consists of 4 fused rings
cholesterol is a steroid, component in animal cell membranes, precursor from which other steroids are built (sex hormones)
high levels in blood = contributes to cardiovascular disease
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