chemistry of life

DSFHISYAUIDYG

Covalent Bond

Strongest Bond, electrons shared between two atoms

Non Polar Covalent Bond

Equal sharing

Polar Covalent Bond

Unequal sharing

Ionic Bond

Electrons transferred from one atom to another

Middle Strength Bond

Hydrogen Bonds

Weak bond, electronegative atoms and hydrogen atoms.

Hydrophilic

Water loving, hydrogen bonds, polar, soluble

Hydrophobic

Water fearing, nonpolar, insoluable

High Specific Heat

Lots of energy needed to break hydrogen bonds, resists temperature changes

Water has high heat of vaporization

Lots of energy needed to go from liquid to gas, evaporative cooling

High surface tension

difficult to break the surface of the water due to hydrogen bonds, adhesion and cohesion

ice floats

crystal lattice, less dense than water

sulfur

used in proteins

nitrogen

proteins/nucleic acids

phosphorus

phospholipids and nucleic acids

hydrocarbon

backbone of organic molecules, carbon chains surrounded by hydrogen bonds

functional groups

groups of atoms that bind to the carbon skeleton of an organic molecule to give ins specific properties

hydroxyl

hydroxyl, polar, found in sugars and alcohols

methyl

methyl, nonpolar, found in carbs

carbonyl

carbonyl, polar, found in carbs

amino

amino, charged, acidic, found in amino acids, fatty acids and other acids

phosphate

phosphate, charged, considered acidic, found in phospholipids, dna backbone (hydrocarbon), and proteins

sulfhydryl

sulfhydryl, polar, found in amino acids and acetyl-coa

dehydration synthesis

monomers join together while losing water. building bonds

hydrolysis

monomer is split by adding water. breaking bonds

carbohydrates

CHO (1:2:1)

carbohydrate monomer

monosaccharide forms polysaccharides via glycosidic bonds

carb function

short term energy, structure/support, cell-cell communication

carb examples

sugars (end in ose), starches, cellulose in cell walls

short monosaccharide chains

quick energy, if not used its stored in the liver as a glycogen (animals) or as starch (plants)

long monosaccharide chains

branched, support in cell walls (cellulose, chitin, peptidoglycan)

lipids

cho

lipid monomer

no true monomer, glycerol and fatty acid tails can combine to form polymers through an ester bond

lipid polymer

phospholipid (glycerol, 2 fatty acids), triglyceride (glycerol, 3 fatty acids), steroids

lipid function

long term energy storage, cell membrane

lipid examples

fats, oils, waxes

saturated fatty acids

saturated fatty acid bonds

single bonds between carbons

unsaturated fatty acids

unsaturated fatty acid bonds

at least one double bond, causes a kink

more double bonds

more unsaturatedmo

more unsaturated

more liquid at room temperature

nucleic acid

chonp

3 parts of a nucleotide

phosphate, sugar, base (such as actgu)

nucleic acid monomer

nucleotide to make a polynucleotide via a phosphodiester bond

nucleic acid function

store genetic information or cell energy

nucleic acid examples

dna, rna, atp, adp, amp

antiparallel

run in opposite directions

3’

-oh group (goes down)

5’

phosphate group (goes up)

covalent bond in dna

nucleotide

hydrogen bond in dna

nitrogenous bases

dna nucleotides

adenine, cytosine, guanine, thymine

rna nucleotides

adenine, cytosine, guanine, uracil

proteins

chon

protein monomer

amino acids make a polypeptide chain via a peptide bond

protein function

structure, support, cell communication, enzymes

protein examples

hemoglobin, amylase, growth hormones

how are proteins synthesized (1)

linear chains of animo acids, connected by the formation of peptide bonds between the carboxyl groups in amino acids and amine group

how are proteins synthesized (2)

r groups can be hydrophobic (nonpolar), hydrophilic (polar) or ionic. the interactions determine the structure and function of the group

primary protein structure

primary protein structure definition

sequence of a chain of amino acids

secondary protein structure

secondary protein structure definition

hydrogen bonding of the peptide backbone causes amino acids to fold into a repeating pattern

tertiary protein structure

tertiary protein structure definiton

3d folding pattern of a protein due to side chain interactions

quaternary protein structure

quaternary protein structure definition

protein consisting of more than one amino acid chain (optional)

pyrimidines

cytosine, thymine, uracil

purines

guanine and adenine