Biochemistry Ch 1 - AA, Peptides, Proteins Flashcards
Central Dogma
DNA -> RNA -> Protein
Replication
DNA copies itself
Transcription
DNA copied into RNA
Script for using nucleic acids
Translation
RNA translated into protein
Translating nucleic acids into amino acids
Reverse Transcription
Reverse Transcriptase makes RNA into complementary cDNA
Retroviruses (HIV)
ncRNA
Noncoding RNA, function as tRNA or rRNA within the cell
Skips the last step of translation into protein
Epigenetics
Changes of gene activity
DNA sequence modified resulting in different phenotype but original DNA sequence stays the same
All DNA the same in different cells (muscle vs epithelial) yet they don’t look or act the same
Amino Acid Structure
Carboxyl acid group (HOOC) Amino group (NH3) H atom R group - different in every AA Alpha carbon - center
Enantiomers
Pair of AA that have mirror image of each other.
L-aa (left amino group) (the ones made in humans)
D-aa (right amino group)
Isoelectric point of AA (pI)
Iso=equal. Neither pos or neg charge
Net charges change when H ions are added or removed. Changing pH
Low pH = inc H+ = amine +1 charge (POS AA)
High path = inc OH- = carb group -1 charge (NEG AA)
(pKa1 (amino) + pKa2 (carb)) / 2 = pI
Zwitterion
Hybrid
AA that has a net zero charge
Because NH3 is (+) and COOH is (-) charged
Peptide bond
Connects 2 AAs
COOH looses OH and NH2 looses H creating H2O
N=C
Double bond so can’t move
α - helix (secondary structure)
AA helix where C=O group form a hydrogen bond with N-H group 4 AAs does the spiral.
R groups just stick out
β - pleated sheet (secondary structure)
Antiparallel sheet: AA starts with Carboxyl group and the second AA below starts with Amino group
Symmetrical hydrogen bonds: 1AA + 1 AA
Parallel sheet: both AA start with Carboxyl group.
Unsymmetrical hydrogen bonds: 1 AA binds with 2 AA
N-H + O=C
Tertiary structure
Secondary structures coming together where AA side chains interact with each other
H bonds, ionic bonds, disulfide bonds
Hydrolysis
Breaking the peptide bond