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30 Cards in this Set

  • Front
  • Back
A
Hydrophobic
Ala
Alanine
V
Hydrophobic
Val
Valine
Y
Hydrophobic
Try
Tyrosine
I
Hydrophobic
Ile
Isoleucine
W
Hydrophobic
Trp
Tryptophan
L
Hydrophobic
Leu
Leucine
K
Hydrophilic
Basic
Lys
Lysine
M
Hydrophobic
Met
Methionine
R
Hydrophilic
Basic
Arg
Arginine
F
Hydrophobic
Phe
Phenylalanine
H
Hydrophilic
Basic
His
Histidine
D
Hydrophilic
Acidic
Asp
Aspartate
E
Hydrophilic
Acidic
Glu
Glutamate
S
Hydrophilic
(polar uncharged R group)
Ser
Serine
T
Hydrophilic
(polar uncharged R group)
Thr
Threonine
N
Hydrophilic
(polar uncharged R group)
Asn
Asparagine
Q
Hydrophilic
(polar uncharged R group)
Gln
Glutamine
C
Special amino acid
Cys
Cysteine
(makes stable disulfide covalent bonds)
G
Special amino acid
Gly
Glycine
(fits into very small spaces)
(usually not found inn an alpha helix Unless the helix is crossing a membrane)
P
Special amino acid
Pro
Proline
(makes rigid kinks in protein chain.)
pnuemonic to remember hydrophilic amino acids
RHK DE STNQ

sounds like Rucus of Stink
Pneumonic to remember hydrophobic amino acids
MILFY WAV
Beta sheet
A secondary structure
Quaternary structure
multiple tertiary structures interacting
Primary structure
Actual sequence of amino acids
Secondary structure
Include alpha helix and Beta sheet
Motiff
Grouping of secondary and tertiary structures that make folds. you can find common motifs in many proteins. certain motifs perform common function is different proteins, ie bind to a certain molecule or ion.
Tertiary structure
Groups of secondary structures interacting with eachother to form a domain. this is the most complicated monomeric structur is able to make, after this the peptide bond must stop and you have to get multiple motiffs interacting.
Domain
a grouping of tertiary structures:
Functional" I cleave DNA"
Structural "I am an arm"
Topological"I extend into Cytoplasm"
Alpha helix
A secondary structure
fromed when amino acid sequence forms hydrogen bonds between the carboxyl group and amine hydrogen. One revolution per 3.6 amino acids