chap. 2 Flashcards
macromolecule sizes (smallest to biggest)
1) monomer
2) dimer (2 monomers)
3) oligomer (3-10 monomers)
4) polymer (11+ monomers)
Dehydration synthesis
- binds a monomer to another macromolecule
- one macromolecule loses an H atom, and the other loses an OH, the two bind together and produce a water molecule as a product
hydrolysis
adding water breaks bonds between monomers
what are the four types of macromolecules
carbohydrates, lipids, proteins, nucleic acids
functional groups
small groups of atoms that give properties/functions to the macromolecule
carboxyl groups make compounds…
make compound weak acids
amino groups make compounds…
make compounds weak bases
carbohydrates
AKA sugars
- carbon chain with 2 H for every 1 O
- near immediate energy use & short to medium term energy storage
carbohydrate sizes
monomers: monosaccharides
dimers: disaccharides
oligomers: oligosaccharides
polymers: polysaccharides
Lipids
AKA fats
- lots of C and H, few O
types of lipids and their functions
fatty acids: long term energy storage (monomer name)
phospholipids: form cell membrane
steroids: hormone (signaling membranes)
Nucleic Acids
composed of nucleotides
- store genetic informations
- immediate energy use
- includes DNA and RNA
ATP
- adenosine triphosphate
- nucleotide
- immediate energy release in cells
- breaking bonds of ATP = energy release
- body uses 88lbs of ATP per day
Nucleotide
- monomer of nucleic acids
- made of a nitrogenous base, 5-carbon sugar (ribose or deoxyribose), and a phosphate group(s)
more phosphates = more energy
example: ATP
Proteins
AKA polypeptides
- composed of amino acids
functions: structure, cell signaling, movement, protection, catalysis, etc
amino acids
monomer of proteins
made of a central carbon, amino group (NH2) which is a weak base, a carboxyl group (COOH) which is a weak acid, and a functional group (R-group) which determines the amino acid’s name and function
how are amino acids bound together?
polypeptide chains (aka peptide bonds)
how are peptide bonds formed
formed by dehydration synthesis reaction of COOH and NH2 group of respective amino acids
primary protein structure
sequence of amino acids, determines all other levels of structure
secondary protein structure
partial-folded structures
containing Alpha helices and Beta pleated sheets
caused by hydrogen bonds between amino acids
tertiary protein structure
- 3D shape
- shape determine the protein function
- caused by interactions between R groups
conformation change
a change in protein function
- can be caused by different molecules binding, unbinding
- some proteins only function correctly when they undergo conformational changes regularly
denaturation
if a protein unfolds, losing its tertiary structure due to heat or acid exposure, it loses its function
denaturation is permeant
Quaternary Protein Structure
combination of two different polypeptides
caused by interactions between two polypeptides