Unit 5 Flashcards
Saturated fats
No double bonds in the fatty acid chains
Are solid at room temperature
Are associated with heart problems
Unsaturated fats
Have double bonds
Are liquid at room temperature
Plant fats, oils, cold, water, fish, insects
hydrogenation
Adding hydrogen to compounds
The hydrogen in Hydrogenation removes the double bonds, increasing the melting point (of oil)
There is partial and full hydrogenation
Trans fat
Fats with cis double bond
Unnatural
Increase melting point of oils (turn oil into margarine)
Cis double bond
A chemical bond were two identical groups attached to the carbon atoms of a double bond are positioned on the same side of the bond plane
Phospholipid
Phosphate group head connected to the 2 fatty acid tails by a glycerol group
Amphipathic ( they have a Hydrolific polar side hydrophobic side)
The hydrophobic tails form the inside of the phospholipid by layer of cell membranes
Steroids
Lipids characterized by carbon skeleton with four fused rings
Cholesterol
Is steroid found in animal cell membranes
Important for maintaining proper membrane fluidity
High levels in blood may contribute to cardiovascular diseases
Precursor for human sex hormones, testosterone and estrogen ( building block for steroids)
Proteins
Chains of amino acids folded into functional forms that do much of the work and cells
Protein functions
Enzymes, storage, hormones, contractile, proteins, structure, receptors, transport, defensive, proteins, signaling proteins, communication, many more
Amino acids
Organic molecules with:
central alpha carbon bonded to an amino group(NH2), a Carboxyl group(COOH), a hydrogen and a Variable side chain called an R group
Amino acids
The monomer of protein
Linked together by peptide bond and unbranched chains
Make peptides and proteins ( final functional unit)
Peptide bond
A chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of another molecule releasing a molecule of water
Features that make amino acid side, chains, nonpolar, and hydrophobic, polar, or charged
Non-polar:
Mostly carbon and hydrogens
No electronegative, oxygen or nitrogen at the end of the R group
Hydrophobic
Features that make amino acid side, chains, nonpolar, and hydrophobic, polar, or charged
Polar:
Has electronegative oxygen, nitrogen, or terminal SH in R group
Hydrophilic
Features that make amino acid side, chains, nonpolar, and hydrophobic, polar, or charged
Charged:
Acid – negative
Base – positive
Hydrophilic
R group
An abbreviation for any group in which a carbon or hydrogen atom is attached to the rest of the molecule
Poly peptide formation
Amino acids are linked by covalent bonds called peptide bonds to form poly peptides (These are unique types of bonds between carboxylic acid and amine groups.)
Poly peptides
Are polymers of amino acids
Can be thousands of amino acids long
Have unique linear, sequences of amino acids
Must be folded properly in order to function correctly
Name the four levels of protein structure
Primary, secondary, tertiary, quaternary
Protein structure: primary
The primary structure of a protein is its unique sequence of amino acids determined by DNA sequence
Protein structure: secondary
Secondary structure is found in most proteins, consisting of coils and folds in the polypeptide chain
The coils and folds of secondary structure result from hydrogen bonds between repeating constitutes of the poly peptide backbone
Typical secondary structures are a coil called an alpha helix, and a folded structure called a beta pleated sheet