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central dogma
information storage, processing, and production of working molecules in our cells
nucleic acids
store and transmit information to make functional proteins
DNA
info storage
transcription
carries info from DNA to RNA
RNA
sends info
translation
read info to synthesize a chain of amino acids to form protein
protein
molecule that does the most work/jobs within a cell; made up of one or more polypeptides; functional molecule; organized into 4 structures
amino acids
building blocks that link into polypeptides to form proteins; monomers
polymers
linked monomers
polypeptides
formed by polymers
backbone of protein
made of an amino group (nitrogen), side chain, and carboxyl group
alpha carbon
central carbon atom in side chain, attached to R group and H
r group
part of the side chain that differentiates the amino acids from one another and grants them their diverse functional properties, they vary between each amino acid; attached to alpha carbon
peptide bond
covalent bond that links 2 amino acids together
dehydration synthesis
removed H2O so the peptide bond can be created
basic
amino acids that are positively charged
acidic
amino acids that are negatively charged
disulfide bridge
2 sulfurs linked together, occurs in the amino acid cysteine (when cysteine encounters another cysteine it drops H and creates a bond between sulfides)
positively charged
hydrophilic, basic
negatively charged
hydrophilic, acidic
primary structure
first level of protein structure; sequence of amino acids
N-terminus
terminal where amino acid sequence starts; free amino group
C-terminus
amino acid sequence ends at this terminal; carboxyl group
carboxyl group
COOH
amino group
free, not attached to anything, H2N (Nitrogen)
secondary structure
second level of protein structure; relies on hydrogen bonding between atoms of the backbone
a-helix
“alpha helix;” part of secondary structure; hydrogen bonds form between peptide chains; held together by hydrogen atoms of backbone
B-sheet
“beta sheet;” part of secondary structure; polypeptide chains
tertiary structure
third level of protein structures; determined by interactions between R groups and between R groups and their environment; ionic bonds, hydrogen bonds, dissulfide bridge, Van der Waals/hydrophobic interactions; 3D and contains multiple secondary structures
binding pocket
cavity in tertiary structure and is what gives protein function, if it loses shape, it loses function
quaternary structure
highest level of protein structures; exists when 2 or more polypeptides come together as subunits of a single functional protein; not all proteins have; stick the same way tertiary structures do
nucleic acids
strings of individual nucleotides each containing a 5’-carbon sugar, phosphate group, and nitrogenous base; information molecules; DNA and RNA
phosphate group
has lots of negative charges that interact with water
5’ carbon sugar
simple sugar with 5 carbons in its structure
nitrogenous base
building block of nucleic acids
hydroxyl
hydrogen atom covalently bonded to oxygen atom
DNA
polymer of deoxyribonucleotides; antiparallel double helix held together through complimentary base pairing; directionally runs from 5’ end to 3’ end
phosphodiester bond
bond between 3’ hydroxyl group and 5’ phosphate group; formed from dehydration synthesis; forms backbone of nucleic acids
antiparallel double helix
strands are flipped relative to one another
complementary base pairing
nitrogenous bases bond with corresponding partner (T=A, G=C in DNA)