← side chains that

are 10h12 able at

Physiological pH

pka -8.3
-

PKa -6
-

pka -12.5
-
Amino Acids W/ Non-polar Aliphatic Side Chains
1. Glycine (G) Gly
2. Alanine (A) Ala Glaciers In Alaska Valiantly Locate Isolated Prowlers

3. Valine (V ) Val
4. Leucine ( L ) hell IIe * the more hydrophobic
fly
5. Isoleucine (1) He A. A. are usually found
increases in hydrophobicity
6. Proline ( P ) Pro within the coreotafolded
7. Methionine (M) Met protein ( shielded from
water )
H H
simplest A- A
E.gg
'

CH }

ggg@0nIyn0n-Ch1ralA.A ,cH3
.

⊕ µ ,

H3N E. qqaea.tl
Glycine
⊕ C00⊖
H3N
H CH3 isoleucine
Has achiral side chain
E. Bg methyl group
( 1-13
⊕ -0
COO
H3N
Alanine structure but
ring
☆ nH" not considered
# \coo⊖

/
aromatic
H CH } µ
R= CHiCH3.CH }
E.gg
-

Hz proline

⊕ coo⊖
H3N
Va cH3
S
H R :
CHZCHZSCH }
CH }
-

"
( Hs E.BG
⊕ -0 tnesisaveryweak
E. AM " 3N
coo
methionine H bond acceptor
-

⊕ COO⊖
H3N I
Leucine in the core
mostly
Amino Acids W/ Nonpolar Aromatic Side Chains
1. phenylalanine (F) The Aroma Of Fine Pine AND * very hydrophobic
2. tyrosine (4) Yellow Timber are

3. tryptophan ( W ) worth thetryp

* phenylalanine ,
along with Valine ,

leucine ,
and isoleucine .is one of the
R :-( 1-1261-15
most hydrophobic amino acids

.q§H2
④ -0
COO
H3N
phenylalanine

OH * tyrosine and tryptophan have hydrophobic

character aswell , butts tempered by the

polar groups in their side chains

.q§Hz tyrosine canionlleatahlghptl

*

-10.1
-

④ -0
COO
" 3" and
tyrosine
*
tyrosine tryptophan
absorb Urat 280hm

HN

E. qBH2
④ -0
COO
H3N
tryptophan
 Amino Acids W/ Polar Side Chains
1. Senne ( s ) Ser H bonds with
*
they can form multiple water

2. Threonine ( T ) -1hr molecules

3. Asparagine ( N ) Asn * these
often found
5 are on the surfaces of
4. Glutamine (a) Gln proteins ( hydrophilic )
5. Cysteine (c) Cys
Stllsaweaktl bond acceptor /
-
donor

1-10 SH side chain can

H H lonlzeatmod .

E. BY E. BY high pHñ8.3
④ -0 ④ -0
COO COO
1-13" serine " 3"
cysteine
HO
cH3
Chiral
qq+ÉaH
"
side
E. chain
④ -0 * the oxidation of two cysteine side
coo
H3N Threonine chains yields a disulfide bond

0
NHZ
H

÷•q• not coded for

④ -0 → by DNA
COO
H3N
Asparagine

NHZ

H 0
E. ago
④ -0
COO
H3N
Glutamine
 Amino Acids W/ Positively Charged ( Basic) side chains
1. Histidine ( H ) His * the basic a- a. are strongly polar ! So they are

2. Lysine ( K) Lys found on the exterior .

3. Arginine ( R ) Arg

•
* Histidine is the least basic of the 3

* * ionizable at pH=6
I

pka-6lsreryclosetophys.IO/O9lcalPH,S0ltHH.N.---=.qq
*

Primarily exists as a neutral species

④ -0
COO
H3N
Histidine

|
⑤
NH3

" " " de "" " "

"

¥900 At physiological pH -7 ,

④
' °O° " " " " " "" " ""

µ ,, thanpkaisothe
Lysine
aminestendtobe

entirely protonated

|µµµgmn {
NHZ ( + charged )
H
←
/ ④ ""2 "" " " " "" " " = ""

÷•q•
④ -0
COO
,
 Amino Acids W/ Negatively Charged ( Acidic ) Side chains

1. Aspartic Acid (D) Asp

2. Glutamic Acid (E) Glu *
typically carry neg Charges at pH ?
.

* negatively charged form predominates

under physiological conditions

*
they are hydrophilic andtendtobeon

the surface Ota protein

|
0

OH

!
pkofsldechain -3.9
-

E. BY At physiological 121-1--7 ,

④ -0 the pills much higher

COO
µ ,µ ynanpka.yen.gg,

aspartame entirely negatively

charged
-
( deprotonated)
o

" Pkofsldecham 4.2

__

¥qq
④ -0
COO
H3N
Glutamic Acid