Bio 4A ch 3

Functional groups are all

• all hydrophilic and reactive except methyl

what are the 4 major macromolecules

1. carbohydrates

2. lipids

3. protiens

4. nucleic acids

monomers

subunits of macromolecules

polymers

monomers linked together via covalent bonds

dehydration synthesis

• 2 molecules of glucose are linked to form the disaccharide maltose

• process of forming polymers from monomers

• water molecule is formed since the 2 monosaccharides are covalently bonded

hydrolosis

• process of breaking polymers down into individual monomers

• add water molecules to break down polymers into their monomeric subunit

whats the difference between dehydration sysnthesis and hydrolisis

dehydration

• BUILDS larger molecules from smaller building blocks

• require energy for forming bonds

• byproduct is water

hydrolosis

• BREAKS down larger molecules into monomers

• releases energy from breaking bonds

• reactant is water + molecule you’re breaking down

enzymes

• biological molecules that catalyze or “speed up” reactions like dehydration and hydrolysis

• specific ones exist for each macromolecule

• end in “-ASE”

carbohydrates

• provide energy to the body in the form of glucose

• found in grains, fruits, and vegatbles

what are the three main subtypes of carbohydrates

1. monosaccharides

2. disaccharides

3. polysaccharides

monosaccharides

• can be linear or ring

• alpha or beta positions

What are the bonds between monocaccharides called?

glycosidic bond

what are the three structural isomers of a hexose monosaccharide

1. glucose - important source of energy

2. galactose -milk/sugar

3. fructose - fruit

glucose, galactose, and fructose are all geometrical isomers T/F

False → they are structural isomers

disaccharide

• form when 2 monosaccharides are linked in a dehydration reaction

• two monomers joined by glycosidic bond

• water is released

  • EX: maltose, lactose, sucrose

polysaccharides

• long chain of monosaccharides joined by glycosidic linkages

• branched or unbranched

• EX: starch, glycogen, cellulose, chitin

chitin

• exoskeleton of arthropods is composed of the polysaccharide chitin

• nitrogen is foiund in it that’s not found in the other types of carbohydrates

Ribose are also known as

pentose

lipids

diverse groups of nonpolar hydrocarbons (hydrophobic)

what are 4 funcitons of lipids

1. long-term energy stores

2. provide insulation ffrom enviornemnt for plants and animals

3. building blocks for some hormones

4. important component of cellular membranes

what are some types of lipids

• fats

• oils

• waxes

• phospholipids

• steroids

what are 2 main components of fats

1. glycerol

2. fatty acids

Triacylglycerol

formed by joining 3 fatty acids to a glycerol backbone through an ester linkage

What are the components of triglycerides?

1 glycerol + 3 fatty acids

saturated fatty acid

• no double bonds

• tightly packed at room temperature

  • butter

unsaturated fatty acid

• 1+ double bonds

  • monosaturated fat = 1 double bond

  • polysaturated fat = 1+ double bond

• Not tightly packed because double bonds cause a kink

  • oils

Cis fats

• H on same side

• kink in chain

  • can’t be packed tightly → liquid

trans fats

• H on opposide side

• no kink

essential fatty acids

required but not synthesized from body so has to come from diet

waxes

• long fatty acid chains linked to long chain alcohols

• hydrophobic

phospholipids

• molecule with 2 fatty acids and modified phosphate group attached to a glycerol backbone

• head = hydrophilic

  • 1 glycerol group

  • 1phosphate group

• tail = hydrophobic

  • one tail has kink (unsaturated)

  • one tail is straight (saturated)

phospholipids are major constituents in what

plasma membrane

steroids

• ring structure

• hydrophobic (nonpolar)

• cholesterol is the most common one

• synthesized is liver

what are 4 functions of steroids

1. Plasma membrane fluidity

2. Precursor to hormones like estrogen and testosterone

3. Precursor to vitamin D

4. Precursor to bile salts

what are 6 functions of proteins

1. Regulatory functions

2. Structural functions

3. Protective functions

4. Transport

5. Enzymes

6. Toxins

what are 3 types of enzymes and their function

1. catabolic → breakdown substrates

2. anabolic → build more complex molecules

3. catalytic → affect the rate of reaction

amino acids

• monomers that make up proteins

• represented by a single uppercase three letters or letter

  • EX: Valine = Val or V

whats the number of amino acids commonly found and how much of that are essential

• 20

• 9 are essential

What type of bonds link amino acids together to form polypeptide chains?

peptide bond (dehydration synthesis reaction)

polypeptide

chain of amino acids joined together in peptide linkages

protein

a polypeptide or multiple polypeptides

protein shape is based on what 4 levels of structure

1. primary structure → linear sequence of amino acids linked by peptide bonds

2. secondary structure → formation of alpha and beta-plated sheets

3. tertiary structure → 3D shape

4. quaternary structure → multiple polypeptide chains

primary structure

• unique sequence of amino acids in a polypeptide

• amino acid sequence is based upon gene encoding that protein

  • a change in nucleotide sequence of DNA could lead to a change in amino acid and lead to change in protein structure and function

  • EX: sickle cell anemia

secondary structure

• local folding of the polypeptide; folding is a result of H bonds

  • alpha helix

  • beta-pleated sheet

tertiary structure

• the unique 3D structure of polypeptide

• due to interactions between R groups on amino acids

quaternary structure

• interactions between several polypeptides that make up a protein

• all 4 bonds are possible

denatureation

• changes in protein structure that lead to changes in function

• can be reversible or irreversible

• can be due to changes in pH or temperature

nucleic acids

constitute the genetic material of living organisms

what are the 2 types of nucleic acids

1. DNA

2. RNA

what are 4 locations of nucleic acids

1. Nucleus of eukaryotic cells

2. Mitochondria

3. Chloroplasts

4. Prokaryotic cells (not membrane enclosed)

Prokaryotes keep their DNA inside the nucleolus T/F

false

chromosomes

• unit of DNA

• contains chromatin

chromatin

complex of DNA and histone proteins (in eukaryotic cells)

what is the main role of RNA

protein synthesis

what are the 4 types of RNA

1. Messenger RNA (mRNA) – a nucleic acid that leaves the nucleus and contains blueprint for protein synthesis (transcription)

2. Transfer RNA (tRNA) – a bridge between nucleotides and amino acids (translation)

3. Ribosomal RNA (rRNA) – assists in protein synthesis

4. microRNA (miRNA) -

FIRST 3 ARE USED IN PROTEIN SYNTHESIS

DNA and RNA consist of monomers known as what

nucleotides

what are the 3 parts of nucleotides (familiarize)

1. nitrogenous base

2. pentose sugar

3. 1+ phosphate group

what are the 2 types of nitrogenous bases

1. pyrimidines (CUT)

   1. cytosine, thymine, uracil

2. purines (AG)

   1. adenine, guanine

what are the 2 types of pentose sugars

1. deoxyribose (found in DNA)

2. ribose (found in RNA)

what are the bases in DNA and RNA

1. DNA → A, T, G, C

2. RNA → A, U, G, C

Example of transcription in DNA

• 5’ C G A T 3’

• 3’ G C T A 5’

what 2 things make up ribosomes

1. proteins

2. rRna

key features of DNA and RNA

DNA → RNA → Protein

• DNA → RNA (TRANSCRIPTION)

• RNA → Protein (TRANSLATION)