Chapter 5 Study Guide s2

Chapter 5 Study Guide

4 major groups of macromolecules

carbs, nucleic acids, proteins, lipids

dehydration vs. hydrolysis

what happens in each

when each is used

dehydration is used in polysaccharides, lipids, and proteins

a water molecule is removed

hydrolysis breaks a water molecule apart and its parts become attached to monomer. Breaks apart fats, proteins, and polysaccharides

steroids have multiple rings, with functional groups sticking out

chemical formulas and molecular structures for all carbs , lipids (3 types), proteins (primary and secondary structures)

carbs have a CHO ratio of 1:2:1, can tell molecular structure by numerous –OH

lipids have a CH ratio of 1:2, and only 2 oxygens, molecular structure has numerous C-H bonds

protein molecular structure – look for amino and carboxyl functional groups

monosaccharide, disaccharide, polysaccharide

number of molecules

examples of each type

mono- 1 molecule, glucose, fructose

di – 2 molecules, lactose

poly – many, cellulose, starch, chitin

starch vs. cellulose

why can’t humans digest cellulose

polymers of glucose

starch stores energy, alpha glycosidic linkages

cellulose used for structural purposes, beta glycosidic linkages

can’t digest b/can’t break down beta glycosidic linkages

facts about lipids

insoluable in water

makes components of cell membrane

stores 2x as much energy as glucose

triacylglycerol

made of 3 fatty acids and a glycerol

saturated fatty acid

no C-C double bonds

unsaturated fatty acid

one or more C- C double bonds

hydrogenation – what it does

decreases# of C-C double bonds

increases # of H atoms

at room temp, goes from oil to solid

saturated fatty acid vs. unsaturated fatty acid

solid at room temp / liquid at room temp b/c double bonds make kinks in structure

polypeptide

polymer of amino acids

parts of an amino acid

amino group, carboxyl groups, H, central carbon, and R group

what makes amino acids different from one another

The R group, or side chain

types of R groups ( polar, nonpolar, basic, acidic, hydrophobic, hydrophilic)

Hydrophobic R groups contain mostly C and H

peptide bonds – where formed

formed between carboxyl of one amino acid and the amino group of the next amino acid, one molecule of water is removed during bond

N terminus vs. C terminus

N – side by amino group

C- side by carboxyl group

Bonds in primary, secondary, and tertiary structures

Alpha helix, beta pleated sheets – where found

When are the interactions of R groups important

Purpose of disulfide bridges

Primary structure – peptide bonds

Secondary structure – hydrogen bonds, alpha helix, beta pleated sheets

Tertiary – 3-D shape of fully folded polypeptide

Disulfide bonds help maintain 3-D shape

Interactions of R groups happen at tertiary level

What happens to protein when 1 amino acid is changed

It can change primary and tertiary structures, and biological activity

Altering any of the structures can change the function of the protein

Examples of protein molecules form 5.4

Hemoglobin

Collegen

Transthyretin

lysozyme

Denaturation – what is it, what structure does it affect

A change in a protein’s 3-D shape or conformation due to disruption of H bonds, Ionic bonds, or disulfide bridges

Chaperonins

Molecules that insure the proper folding of a protein

Function of RNA

Function in the synthesis of protein

Pats of a nucleotide

5 carbon sugar, nitrogenous base, phosphate group

Purines vs. pryamidines

Purines – adenine and guanine, 2 rings

Pyramidiens – thymine, cytosine, uracil, 1 ring

A-T G-C

DNA bases vs. RNA bases

DNA – A, T, G, C

RNA – A, U, G, C

Differences between DNA and RNA

DNA - two strands, deoxyribose sugar, one less O than RNA

RNA – one strand, ribose sugar

What bonds hold the two sides of DNA together

Hydrogen bonds