Amino Acids & Proteins Flashcards
Amino acids contain amino (NH2) and carboxyl (COOH) identified by their _____
Side chain
The 20 standard amino acids are ‘standard’ because they are _____, meaning they are used to build polypeptides and proteins
Proteinogenic
All amino acid are in L-configuration. True or false
False. Cysteine is in S-configuration
List the essential amino acids
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List the non essential amino acid
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Amino acids essential for infants
Histidine
Semi-essential amino acid
Arginine
Simplest amino acid
Glycine
Side chains of amino acid cane be which of the following:
A. Alkyl group
B. OH or S group
C. Carboxyl group
D. Basic
E. Aromatic
ABCDE
Recall the 20 standard amino acids noting their 3- and 1- letter code
Alanine
Ala
Α
Arginine
Arg
R
Asparagine
Asn
N
Aspartic acid
Asp
D
Cysteine
Cys
C
Glutamic acid
Glu
E
Glutamine
Gln
Q
Glycine
Gly
G
Histidine
His
H
Isoleucine
lle
I
Leucine
Leu
L
Lysine
Lys
K
Methionine
Met
M
Phenylalanine
Phe
F
Proline
Pro
P
Serine
Ser
S
Threonine
Thr
T
Tryptophan
Trp
W
Tyrosine
Tyr
Y
Valine
Val
V
In amino acid’s characteristic titration curve, the predominant species in low pH is fully protonated form. True or false
True
First stage of titration corresponds to the removal of the proton from _____. The sceond stage is the removal of proton from _____.
COOH, NH3^+
____ is reached when the removal of first proton is completed and the removal of second proton has begun
Inflection point
pH at the inflection point. The characteristic pH at which the net electric charge is zero
Isoelectric pH
Point where the amino acid exist in zwitter ionic form
Isoelectric point
Amino acid are linked together by a covalent bond between amino group of one AA and the carboxylic group of the next amino acid. This linkage is called _____
Peptide bond
Formed by polymerization of amino acids
Polypeptides
When amino acid are used in the peptide bond formation, each amino acid is called ____
Residue
When polypeptides are properly folded and completely functional, they comprise a _____
Protein
Amino acids that can disrupt alpha helices
Glycine and Proline
Sequence of AA which comprise a polypeptide chain
Primary structure
alpha helices and beta pleated sheets
Secodnary structures
Secodnary structures of AA are stabilized by ____ between NH2 and COOH of non adjacent AA
H-bonds
Peptide bond is an amide bond
True
Three dimensional shape of polypeptide.
Tertiary structure
The unique stabilizing interaction in the teriary structures
Dislfide bridges
Assembly of peptide chains to functional protein complex
Quaternary structure
Classification of protein that are relatively spherical or ovoid in shape, functional purpose, irregular AA sequence, sensitive to pH and temp changes. Includes enzymes, hemoglobin, and insulin
Globular protein
Classification of protein that are long and narrow in shape, structural purpose, repetitive AA sequence, less sensitive to pH and temp changes. Includes collagen, keratin, actin, myosin, elastin
Fibrous protein
In terms of solubility, ______ proteins are generally insoluble in water whereas _____ proteins are generally soluble.
Fibrous, globular
Efers to the modification in the secondary, tertiary, and quaternary structures of protein without rupture of the peptide bonds in the primary structure
Denaturation
Experiment that proves the possibility of denaturation
Alfinsen’s experiment
