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67 Cards in this Set

  • Front
  • Back

carbon containing comppunds

almost all molecules a cell makes

Variation of carbon skeletons

length ~ double bonds ~ branching ~ rings

Properties of organic compinds depend on

size and shape ~ atoms attached

Most important chemical groups

hydroxyl, carbonyl, carboxyl, amino group, phosphate, methyl

Which does not contain carbon?

Amino, hydroxyl, phosphate

Four main classes of macromolecules

carbohydrates, lipids, proteins, nucleic acid

Difference of lipids from others.

Not soluble in water

small molecules joining together in chains

polymers

building block of polymers

monomers

connects monomers

dehydration reaction

disassemble monomers

hydrolysis

give range of monomers that molecules vary

40 - 50

diversity comes

from linear sequences and thousand different macromolecules

Carbohydrates contain

carbon, oxygen, hydrogen

simple sugars

monosaccharide

double sugars

disaccharides

complex sugars

polysaccharide

trademarks of sugars

hexoses

Functions of sugars.

major nutrients ~ source of energy ~ raw materials

glucose + glucose

maltose (beer)

glucose + fructose

sucrose (table sugar)

Types of polysaccharides.

Storage ~ structural

Storage

starch (plants, glucose, leaves and stem)


glycogen (animals, glucose, muscle, liver)

Structural

Cellulose (cell wall plants)


Chitin (exoskeleton animals)

Lipids mixes

poorly with water

Types of lipids

Fats ~ phospholipids ~ steroids

Compromises fats

glycerol ~ fatty acids

Major functions of fats

energy storage

Phospholipids essential for

making up of cell membrane

Describe composition of phospholipids

Hydrophilic heads ~ hydrophobic tails

Phospholipids added in water?

Double layered structures called "bilayers"

Steroids

Four fused rings

Sex hormones

Cholesterol

Proteins came from Greek word

"proteios" primary or first

Compromises % of cell dry mass

50%

Types of Functions in proteins

enzymatic ~ storage ~ defensive ~ transport ~ hormonal ~ contractile and motor ~ receptor ~ structural

coordination of organism activities

hormonal (insulin)

protects against disease

defensive (antibodies)

accelerate chemical reactions

enzymatic (digestive)

support

structural (keratin)

stores amino acids

storage

transport substances

transport (hemoglobin)

response to stimuli

receptor

movement

contractile and motor (actin, myosin)

Composition of amino acids

carboxyl ~ amino ~ r group ~ hydrogen

Different types

nonpolar (hydrophobic)


polar (hydrophilic)


electrically charged (+-)

peptide bonds are made through

dehydration reaction

amino end, carboxyl end

N-terminus, C-terminus

specific activities results from

intricate three dimensional architecture

single polypeptide folds and coils to form

functional protein

Two models

Ribbon ~ space filling

Four levels of protein structure

primary ~ secondary ~ tertiary ~ quaternary

hydrogen bonding causes folding

seondary

more than one amino acid chain

quaternary

sequence of a chain in amino acids

primary

3 dimensional folding, side chain interactions

tertiary

monomers of nucleic acid

nucleotides

Two types

RNA, DNA

what makes up nucleotide

pentose sugar ~ phosphate group ~ nitrogenous bases

two types of pentose

deoxyribose ~ ribose

Two types of bases

Purine (two rings)


Pyrimidine

Examples of purine

Adenine ~ Guanine

Examples of Pyrimidine

Thymine ~ cytosine ~ uracil

# of polynucleotides RNA

single

# of polynucleotides DNA

two (double helix)

name of backbone

sugar phosphate backbone (complementary bases)

Relationship of DNA and RNA

DNA sorted info ~ before synthesis, copied in another type called mRNA