AP E1: Organic Molecules of Life

Created by jennifernewwin 

Upgrade to
remove ads

43 terms

Hierarchy of complexity

Atoms, molecules, organelles, tissue, organs, organ systems, organism

Monosaccharides

glucose, galactose, fructose

Disaccharides

sucrose, lactose, maltose

Sucrose

glucose + fructose

Lactose

glucose + galactose

Maltose

glucose + glucose

Plant polysaccharides

starch (amylose- used for energy storage; humans CAN digest) and cellulose (used for structural support and what humans CAN'T digest---humans use it as fiber instead)

Animal polysaccharides

glycogen used for energy storage and is stored in our liver and muscles. When we go on diets, we lose a lot of weight at first because we are burning out glycogen storage. More sedentary = more glycogen storage.

Dehydration synthesis

small things come together to form big thing by REMOVING WATER. Anabolic, endergonic, decreases energy because you have to put energy into them. I.E. triglyceride synthesis or polymerization of amino acids

Hydrolysis

breaking big thing into small things by ADDING WATER. catabolic, exergonic, release energy

Carbohydrates

used for energy and energy storage, cell-cell recognition; hydrophillic.

Types of Polysaccharides

starch, cellulose, and glycogen. made by long chains of glucose.

types of conjugated carbohydrates

glycolipids, glycoproteins, proteoglycans. HELD BY COVALENT BONDS.

Glycolipids

found on external surface of cell membrane. carb + Lipid

Glycoproteins

external surface of cell membrane, mucus of respiratory and digestive tract. used in goblet cells which secrete the glycoprotein mucin which absorbs water to form mucus. CARB + PROTEIN.

Proteoglycans

like glycoprotein except the CARB portion is MUCH LARGER than the protein section. Macromolecule used for cell adhesion, gelatinous filler of tissues and lubricants joints. Gives connective tissue high compression strength.

Lipids

Hydrophobic. Less oxidized than carb but contains more calories per gram.

Types of lipids

fatty acids, triglycerides, phospholipids, eicosanoids, steroids.

Fatty Acids

a methyl group at one end and a carboxyl group at the other. Saturated fatty acids contain no double bonds while unsaturated fatty acids contain double bonds. Saturated fats are solid at room temperature because more tightly packed and have greater attraction to each other.

Triglycerides

Function primarily as energy storage, insulation and cushion. Old people lose triglyceride fat so that's why we can see veins really clear in hands.

Synthesis of Triglycerides

With the help of lipase enzyme, dehydration synthesis between a glycerol and 3 fatty acids. Hydroxyl groups of glycerol bind with the carboxyl end of the fatty acids. Called neutral fats because their carboxyl group merge with the hydroxyl groups of the glycerol molecule making them no longer acidic.

Phospholipids

Amphiphilic due to the phosphate group and the two fatty acids. Basis of phospholipid bilayers with fatty acids in the inside and phosphate group on the outside.

Synthesis of phospholipids

Glycerol + two fatty acids + phosphate group. PHosphate group = highly polar, electronegative, and hydrophilic. Fatty acids = hydrophilic.

Eicosanoids

derived from a fatty acid and used to help us perceive pain, blood cloting, labor contractions, blood vessel diameter, and chemical messenger.

Steroids

Derived from cholesterol, a type of steroid. Made up of 4 rings. Makes up 20% of the cell membrane. Produced only by animals. Required for proper nervous system function.

Cholesterol

Makes up 20% of the cell membrane. Produced only by animals. Required for proper nervous system function. Stored in liver. Important for transport, sex hormones, estrogen, progesterone, glycocorticoids, ect. They can fit through the cell membrane and can act directly on DNA /transcription.

Proteins

Made up of amino acids. 20 types of aa known. Amino acid made up of R-group, carboxyl group, amine group, and a hydrogen. R-group is responsible for whether or not aa is polar or nonpolar. Proteins are usually amphiphilic.

Synthesis of proteins

via dehydration synthesis between hydroxyl group of carboxyl group and hydrogen of amine group to produce a peptide bond.

Primary structure of AA

order of amino acids

Secondary structure of AA

alpha helix or beta sheet fromed by hydrogen bonding between C=O and hydrogen of amino group. Beta sheet leads to silkier feeling while alpha sheets lead to more course, wool-like feel.

Tertiary structure of AA

Folding due to R-group interactions via H bonds or disulfide bonds.

Quaternary structure of AA

interactions between 2+ polypeptide chains via H bonds or disulfide bonds. Ex. insulin or hemoglobin.

Conjugated proteins

Protein + something else (aka a moiety). Like in Hemoglobin.

Protein denaturation

ALthough normal protein function involves small conformation changes, major conformation changes results in denaturation and loss of protein function. Occurs with pH and heat; With pH, you get denaturation occurring with too much acid and base, however with temperature, denaturation only occurs with high temperatures (only one side).

Protein denaturation by pH

Proteins lose function more easily with acid than base because protons (acids) are smaller and faster than bases (HCO3-) and thus acids can get to the protein faster and mess things up better than bases. Optimal pH - depends on where in the body.

Protein denaturation by heat

Proteins lose more function when it gets really really hot than cooler temps because at really hot temperatures, the amount of KE added is too much and allows for the bonds to be broken more easily. Optimal temp - body temp.

Protein functions

structure, comm. , membrane transport, catalysis, recognition and protection, movement, and cell adhesion. NOT ENERGY bc 1.) protein enzymes can't distinguish between body protein and food protein. 2.) Only occurs during starvation.

Enzymes

used as catalysts to speed up exothermic reactions (high to low energy) by lowering the activation energy. composed of a protein and non protein (cofactor) portion. Work by slightly changing the shape of the substrate; however not consumed by reaction.

Enzyme functionality

highly specific (acts only on one substrate and only speeds up one rxn), very efficient, under nuclear control.

Cofactors

minerals, inorganic molecule that binds to an enzyme to help it function (change its shape/create active site). Ex. iron, cu, zn, mg, ca.

Coenzymes

organic molecules aka vitamins.

Function of cofactors and coenzymes

bind allosterically; they bind somewhere other than the active site which leads to a change in the active site shape.

Galactosemia

Infant can't break down galactose leading to high blood sugar but no pathway to make them feel hungry. Thus leading to anorexia. Treatment is to get rid of milk from diet.

Please allow access to your computer’s microphone to use Voice Recording.

Having trouble? Click here for help.

We can’t access your microphone!

Click the icon above to update your browser permissions above and try again

Example:

Reload the page to try again!

Reload

Press Cmd-0 to reset your zoom

Press Ctrl-0 to reset your zoom

It looks like your browser might be zoomed in or out. Your browser needs to be zoomed to a normal size to record audio.

Please upgrade Flash or install Chrome
to use Voice Recording.

For more help, see our troubleshooting page.

Your microphone is muted

For help fixing this issue, see this FAQ.

Star this term

You can study starred terms together

NEW! Voice Recording

Create Set