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a
bunch
of
losers;
to
my
as
relate
amine
I
car
0
·
amino acid+
t
zen
amino
acid
carboxylic
acids
that have an amino
group
real
structural
formula
H
Ho
this variation
know
11
ur H
N C C OH
give
character
basics
I
carboxyl
I
-stic properties
is
amino
R
grOUP
group
side
the
set
2-amino acids
grou
20
diff (
20
standard amino
acid
the only
20
it
alkyl group none,
H alkyl group alkyl group rigid cyclistructure alkyl group
X X X
aromatic group indole
Phenolic-olgroup carboxylicacid carboxylicacid guanidinogroup
imidazolering
X X
amino group
hydroxyl sulfide amide amide
X- not
withinsas; a
bus
miy
as
physical
properties
form a
>
amino acids has: dip
ofar
ion or
·
carboxyl
(-100H)
group
(acidic
groups)
internal
I
Salt
·
amino
(-NH2)
group
(basic
group)
called
zwitterion
molecules with a
positive
charge
zwitter
on one atom and
a
negative charge
X
on another atom
whereby
the molecule
Don
has no net
charge.
H
H O
I
H2N
C C
OH
H3N
C
co
R
(no
net
charge)
R
zwitterion form is the
natural
state
in
which the
amino acid
exists.
4
so,
amino acids
exhibit
properties
similar to salt:
amino acids
are
crystalline
solids with
melting
point
soluble in
water
insoluble
in
non-polar
organic
solvent
large
dipole
moment
high
dielectric constant
value
miy
as
reactions
of
amino
acid
(have
e
carboxylic
acid
GrOUP
and
acid)
I reaction
with NaOH
NaOH
(salt-water
H3N
CH
-o- +
NaOH
HaN
CH
-ONa+
HaO
reaction with alcohol cesterification)
a.a
alcohol""> ester-water
HEN
CH
-o-+ROH
HCl> HaN
CH-OR
+HOO
amino
group
and
bases)
reaction
with
HC
HC
>aminium salt
C
HEN
CH
-o
-+
HC
H3N
CH-OH
reaction
with acid
chlorides
a.a
acid
chlorides
(acyl
derivatives
0
O
I
HEN
CH
I
-o
mic
>R
C
HN
CH
o-tHC
reaction with nitrous acids
a.
nitrous
acid
x
hy
0 carboxyl
Yid
HEN
CH
-O-HONOHOL
HO
CH
COOH+
Cl
CH
COOH
0°C
CH20H
CH
CH
CHz
=
CH-C00H
mily
as
peptides
felimination
under suitable
condition, of
water
molecule
acid + amine>amide
H
condensation
reaction
4
When amino
acid are
joined together
by
amide bonds
form
larger
molecules
called
peptides
and
protein
polypeptides
I
have
many
amino
acid
joined together
in
long
linear chains
>
protein
the
term
reserved
for
polymers
of more than
amino
acids
peptide
bond
special
name
given
tothe amide
bond
formed between
amino
group
of one
a-amino acid and the
x-carboxyl
group
of
another
x-amino
acid
amino acid
residue
4 the
individual amino
acid
amide
linkage
dipeptide
2 a.9 units
a-carboxyl X-amino
tripeptide
group
O
↑
group
O 3 a. units
X 11
another
11 another
S
amin o
C
N
amino C
N
units
miy
as
peptide
x-carboxyl <-
amino
bond
grou
O
↑
group
O
I
X I another
11
H,N
amin o d-o
HN amino c
acid
2
acid
miyas
dum
dum
H
explaination moment:
(N-terminal)
(C
terminal)
V
resonance
trans
O
UP
resonance,
no
I
X 11 another
iP
matter
Wut,
C-N bond H,N
am
in o
C
N amino c-
H
acid acid
sentiasa 1800
or
I H
Or
=
(straight)
3
x
kisah HIN-
peptide
(-CONH-C
COOH
a.d cantum
type
linkage linkage
1800>
long
chain
6
possible
H H
variation
N N
tide
Cr
00
S -
C
I
of
pep
A
having
bond:
sO
te
0
this
makes
13
R
C
N
&
india a
significant
H resonance
R
change
to
0
G
the
hybrid
asM
c
N
Y
R
do >R
N
0
00 I
C R
C
H
3)R
c
N
A
⑧
· 08 R
08
R
R
R
I
R
trans (morestable)
R
&
CiS
0
C
N
H
R
I ~O
N C
consequences
of
resonance
in amides
H
R
H 6)R
N c
0
4
rotation in C-N
is]
mama
ge
n(
restricted
bond (7)
R
H
R
4
the bond
is
stronger
3
cuz partial=)
ja
R
trans
(miyass
all amide variations involved
120:
1800
in
peptide
bond lie in the
same plane
(so akan cantum meman;
ang)
result
of
theseeffects in
a
long
peptide
chain
4 the trans
arrangement
makes
the
long
chain
(inzigzag)
4 in each
peptide bond,
N-H and
c=
bonds lie
parallel
H I
C
N
N
C
N
H
0
OH
NHS
C
I
c
d
C
↓
d!
a
C-terminal
N-
I
-R
H
RI
↓x
amino
acid residue
terminalend R
akan dudukcelah-CONH-
miy
as
prOfell
boyamides
containing
from
40 to
several
thousands
amino acid
residue
4
vary
greatly
in
composition
and in structure
4
each
protein
has its own and
composition
4 the
sequence
of a 9
in the
protein
molecule
determine the
shape
and function
hydrolysis
of protes
boiling
with
dilute mineral
acid (eXp:
H21)
protein
H
, amino
acids boiling
with
7
(exp.
N9OH)
an
alkalilag)
can
be
rehydrolyzed
to reform
a
a)
action of
enzymes
at 40°
structure
of
proteins
primary
particular sequence
of 9.9 that
is
structure
joined together
by peptide
chain
or
protein
the most
important
element:amide
bond,
covalent,
bond
although
CONH-Camide
bond)
is
restricted,
the
side R in
protein
backbone
is not.
secondary
the
shape
of
the
protein molecule caused
by hydrogen
bonding
between-c=
structu re and -N-H
grOUPS
1-CONH-
+WO -ne/iX
B-pleated
sheet
main:
x
peptide
peptide
snape
bond bond
~
.. .
-.
z
v
--
V
W
--
~a
~
