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64 Cards in this Set

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Carbon Formations
1. forms covalent bonds, needs 4 electrons per octet rule.
2. Carbon-Carbon & Carbon-Hydrogen are non-polar.
3. Hydrocarbons tend to be poorly soluble.
4. Polar covalent bonds with oxygen or nitrogen are soluble.
5. Stable at different temperatures associated with life.
Function Groups
Groups of atoms with special chemical features that are functionally important. Exhibits the same properties in all molecules.
ex. Amino, Carboxyl, Methyl, Phosphate
Isomers
Two Structures with an identical molecular formula but different structures and characteristics.

1. Structural
2. Stereoisomers
Structural Isomer
contain the atom but in different bonding relationship
Stereoisomers Isomer
identical bonding relationships, but the spatial positioning of the atoms differs in two isomers.

1. geometric
2. enantiomer
Geometric Isomer
CIS - if bonds are on the same side
TRANS - if bonds are opposite sides
* both very different chemical properties(stability & sensitivity to head and light)
Enantiomer Isomer
pair of molecules that are mirrored

1. share identical chemical properties( solubility, melting point)
2. due to orientation of atoms in space, their ability to non covalently bond are different.
Polymers
Large molecules that formed by linking together many smaller molecules called monomers.

1. Structures depends on
a. structure of monomers
b. number of monomers linked together
c. 3-D way in which monomers are linked
Carbohydrates
Composed of carbon, hydrogen, and oxygen atoms Cn(H2O)n
1. Sugers
Sugars
Small carbohydrates that taste sweet.

1. Monosaccharides
2. Disaccharides
3. Polysaccharides
Monosaccharides
Simplest sugars. Most common are molecules with five carbons, called pentoses, six carbons called hexoses(glucose)

1.
Glucose
Very water soluble, broken down by enzymes and the energy released is used to make ATP molecules which power many cellular processes. Exists as D & L glucose: mirror images of each other.
Disaccharides
Two sugars. Carbohydrates composed of two monosaccharides.

1. Bond between two sugar molecules is a glycosidic bond.
2. Hydrolysis of a glycosidic bond in a disaccharide breaks by adding back the water and thus uncouples the two.
Polysaccharides
when many monosaccharides are linked together to form long polymers.

1. Starch - found in plants, less soluble
2. Glycogen - Present in animal cells and sometimes called animal starch, higher degree of branching contributes to solubility.
3. Cellulose - Polymer of B- glucose, with a linear arrangement of carbon-carbon bonds.
4. Chitin - a tough, structural polysaccharide, forms external skeleton of many insects and the cell walls of fungi.
Glycosaminoglycan
large polysaccharides that play structural roles in animals
Lipids
Molecules composed of predominantly of hydrogen and carbon atoms. Non-polar and therefore very insoluble in water. 40% of organic matter in human body.

1. Fats
2. Phospholipids
3. Steroids
4. Waxes
Fats
Mixture of triglycerides. Formed by glycerol to three fatty acids. A fatty acid chain is made up of carbon and hydrogen atoms with a carboxyl group at the end.

1. Saturated
2. Unsaturated
Ester Bonds
Each of the three hydroxyl groups in glycerol is linked to the carboxyl group of a fatty acid by the removal of a molecule of water by dehydration reaction.
Synthesis of Fatty Acids
synthesized by linking together two-carbon fragments
Saturated Fatty Acids
When all carbons in a fatty acids are linked by single covalent bonds. High melting point, solid at room temperature.
Unsaturated Fatty Acids
One or more C=C double bonds. Low melting points, liquid at room temperature.

1. Monosaturated Fats - One C=C bond
2. Polyunsaturated Fats - Two or more C=C bonds
Fatty acids and Energy
Can be metabolized to provide energy to make ATP.
Phospholipids
similar in structure to triglycerides except the third hydroxyl group of glycerol is linked to a phosphate group instead of a fatty acid.

1. Small polar or charged nitrogen-containing molecule is attached to phosphate. Constitutes a polar hydrophilic region.
2. Fatty acid chain provides a non-polar hydrophobic at the opposite end.
3. In water, when phospholipids become organized into bilayers, their non-polar ends face each other while the polar ends are attracted to water molecules.
Steroids
Have a distinctly different chemical structure from that of other types of lipid molecules. Four fused rings of carbon atoms form the skeleton of steroids.

1. Estrogen differs from testosterone by having one less methyl group, a hydroxyl group instead of a kelone group, and additional double bonds in one of its rings.
Proteins
composed of amino acids.
Amino Acids
Contain carbon, hydrogen, oxygen, nitrogen, and small amounts of other elements. The building blocks of protein.
Amino Acid Structure
a α-carbon is linked to an amino group and a carboxyl group. The α-carbon also is linked to a hydrogen atom and a side chain.
Amino Acid Solubility
When dissolved in water, the amino acid group accepts a hydrogen ion and is negatively charged.
Side-Chain
Their structures are critical features of protein function. The arrangement and chemical features cause proteins to fold and adopt the 3-D shapes.
Amino Acid Dehydration
Joined together by linking the carboxyl group of one amino acid to the amino group of another, a molecule of water is formed each time two amino acids are joined by dehydration reaction.
Peptide Bond
The covalent bond formed between carboxyl and amino acid group.
Polypeptide Bond
The resulting molecule when many amino acids are joined by peptide bonds.

1. Refers to structural unit composed of amino acids. In contrast, a protein is a function unit composed of one or more polypeptides that have been folded and twisted into precise 3-D shapes that carry out a particular function.
Hierarchy Structure of Proteins
Levels of structure that are dependent of each other. If one level changes, the others change as well.

1. Primary Structure
2. Secondary Structure
3. Tertiary Structure
4. Quaternary Structure
Primary Structure
its amino acid sequence, from beginning to end determined by genes.
Secondary Structures
Amino acid sequence folded into a more compact structure.

1. α helix - Polypeptide backbone forms a repeating helical structure that is stabilized by hydrogen bonds.
2. β Sheet - Regions of the polypeptide backbone come to lie parallel to each other.
3. Random Coiled Regions - Some regions along a polypeptide chain do not assume a secondary structure, but are very specific and important to the function of a protein.
Teriteary Structure
As the secondary structure becomes established due to the particular primary structure, a polypeptide folds and refolds upon itself to assume a complex 3-D shape
Quaternary Structure
When proteins consist of one or more than one polypeptide chain.
Factors that influence Protein Structure
1. Hydrogen Bonds
2. Ionic Bonds & Polar Attractions
3. Hydrophobic Effect
4. Van der Waals forces
5. Disulfide Bridges
Hydrogen Bonds
The large number of hydrogen bonds within a polypeptide and between polypeptides adds up to a strong force that promotes protein folding and stability.
Ionic Bonds & Polar Attractions
Some amino acid chains are positively charged while others are negatively charged.

1. Positively Charged- May bond to negatively charged side chains via ionic bonds.
2. Uncharged - may interact with ionic amino acids.
Hydrophobic Effect
Likely to be found in the center of the protein to avoid contact with water.
Van Der Walls Forces
Atoms within molecules have weak attractions for each other if they are optimal distance apart
Disulfide Bridges
The side chain of the amino acid cysteine contains a sulfhydroxyl group which can react with a sulfhydroxyl in another cyseine side chain to produce a disulfide bridge or bind which links the two amino acid chains together.
Nucleic Acids
Account for only 2% of weight in animals. Responsible for storage, expression, and transmission of genetic information.

1. DNA
2. RNA
DNA
Store genetic information coded for the sequence of their monomer building blocks.

1. Nucleotides
2. Bases
Peptide Bond
The covalent bond formed between carboxyl and amino acid group.
Polypeptide Bond
The resulting molecule when many amino acids are joined by peptide bonds.

1. Refers to structural unit composed of amino acids. In contrast, a protein is a function unit composed of one or more polypeptides that have been folded and twisted into precise 3-D shapes that carry out a particular function.
Hierarchy Structure of Proteins
Levels of structure that are dependent of each other. If one level changes, the others change as well.

1. Primary Structure
2. Secondary Structure
3. Tertiary Structure
4. Quaternary Structure
Primary Structure
its amino acid sequence, from beginning to end determined by genes.
Secondary Structures
Amino acid sequence folded into a more compact structure.

1. α helix - Polypeptide backbone forms a repeating helical structure that is stabilized by hydrogen bonds.
2. β Sheet - Regions of the polypeptide backbone come to lie parallel to each other.
3. Random Coiled Regions - Some regions along a polypeptide chain do not assume a secondary structure, but are very specific and important to the function of a protein.
Teriteary Structure
As the secondary structure becomes established due to the particular primary structure, a polypeptide folds and refolds upon itself to assume a complex 3-D shape
Quaternary Structure
When proteins consist of one or more than one polypeptide chain.
Factors that influence Protein Structure
1. Hydrogen Bonds
2. Ionic Bonds & Polar Attractions
3. Hydrophobic Effect
4. Van der Waals forces
5. Disulfide Bridges
Hydrogen Bonds
The large number of hydrogen bonds within a polypeptide and between polypeptides adds up to a strong force that promotes protein folding and stability.
Ionic Bonds & Polar Attractions
Some amino acid chains are positively charged while others are negatively charged.

1. Positively Charged- May bond to negatively charged side chains via ionic bonds.
2. Uncharged - may interact with ionic amino acids.
Hydrophobic Effect
Likely to be found in the center of the protein to avoid contact with water.
Van Der Walls Forces
Atoms within molecules have weak attractions for each other if they are optimal distance apart
Disulfide Bridges
The side chain of the amino acid cysteine contains a sulfhydroxyl group which can react with a sulfhydroxyl in another cyseine side chain to produce a disulfide bridge or bind which links the two amino acid chains together.
Nucleic Acids
Account for only 2% of weight in animals. Responsible for storage, expression, and transmission of genetic information.

1. DNA
2. RNA
DNA
Store genetic information coded for the sequence of their monomer building blocks.

1. Nucleotides
2. Bases
Nucleotide
Made up of phosphate group, five carbon sugar, and a single or double ring of carbon and nitrogen.
Base
1. Purine - double fused rings of nitrogen and carbon atoms. Adenine(A), Guanine(G)
2. Pyrimidine - Single ring of nitrogen and carbon atoms. Cytosine(C), Thymine(T)
Helix
Two strands are held together by hydrogen bonds between a purine base in one strand and a pyramidal base in the opposite strand. (A-T, G-C) pairing.
RNA
Involved in decoding this information into instructions for linking together a specific sequence of amino acids to form a polypeptide chain. Consists of a single strand of nucleotides. The sugar is ribose. Contains uracil as pyrimidine base.