Notes Amino Acids and Proteins

Proteins are about 50% of the dry weight of most cells, and are the most structurally complex
molecules known. Each type of protein has its own unique structure and function.
Polymers are any kind of large molecules made of repeating identical or similar subunits called
monomers. he starch and cellulose we pre!iously discussed are polymers of glucose, which in that
case, is the monomer. Proteins are polymers of about "0 amino acids monomers.
he amino acids all ha!e both a single and triple letter abbre!iation. #ere is an example.
$lanine % $ % $la
Each amino acid contains an &amine& group, '(#
"
) and a &carboxylic acid& group '*++#)
'shown in black in the diagram).
he amino acids !ary in their side chains 'indicated in blue in the diagram).
he eight amino acids in the orange area are nonpolar and hydrophobic.
he other amino acids are polar and hydrophilic '&water lo!ing&).
he two amino acids in the magenta box are acidic '&carboxylic& group in the side chain).
he three amino acids in the light blue box are basic '&amine& group in the side chain).
Amino Acids: shown in another structural formula format
C C NH
2
H O
OH
*#
,
C C NH
2
H O
OH
*#
#
,
* *#
,
C C NH
2
H O
OH
*#
"
*#
#
,
* *#
,
C C NH
2
H O
OH
*#
*#
"
*#
,
*#
,
C C NH
H O
OH
*#
"
*#
"
*#
"
alanine valine leucine isoleucine proline
ala A val V leu L ile I pro P
C C NH
2
H O
OH
*#
"
C C NH
2
H O
OH
*#
"
*#
"
-
*#
,
C C NH
2
H O
OH
*#
"
NH
*
C C NH
2
H O
OH
#
C C NH
2
H O
OH
*#
"
+#
phenylalanine methionine tryptophan glycine
*
serine
phe F met M trp W gly G ser S
C C NH
2
H O
OH
*#
*#
,
+#
C C NH
2
H O
OH
*#
"
+#
C C NH
2
H O
OH
*#
"
-#
C C NH
2
H O
OH
*#
"
* +
(#
"
C C NH
2
H O
OH
*#
"
*#
"
* +
(#
"
threonine tyrosine cysteine asparagine glutamine
thr T tyr cys ! asn " gln #
C C NH
2
H O
OH
*#
"
* +
+#
C C NH
2
H O
OH
*#
"
*#
"
* +
+#
C C NH
2
H O
OH
*#
"
(
(#
C C NH
2
H O
OH
*#
"
*#
"
*#
"
*#
"
(#
"
C C NH
2
H O
OH
*#
"
*#
"
*#
"
(#
*
(#
"
(#
aspartic aci$ glutamic aci$ histi$ine lysine arginine
asp % glu & his ' lys ( arg )
$mino acids are named as such because each amino acid consists of an amine portion and a
carboxylic acid part, as seen below.
* * (#
"
# +
+#
.
*ompare this structure to the abo!e structures of each of the amino acids. Each amino acid has this
general structure.
he side chains are sometime shown as ./groups when illustrating the backbone.
0n the approximately "0 amino acids found in our bodies, what !aries is the side chain. -ome side
chains are hydrophilic while others are hydrophobic. -ince these side chains stick out from the
backbone of the molecule, they help determine the properties of the protein made from them.
he amino acids in our bodies are referred to as alpha amino acids. he reason is that the central
carbon is in an alpha position in relation to the carbonyl carbon. he carbon ad1acent to the carbonyl
carbon is designated the alpha carbon. Each carbon in the chain will be designated with a different
letter of the 2reek alphabet. -ee the example below.
*#
+
CH
3
CH
2
CH
2
CH
2
CH
2
alpha
beta
gamma
delta
epsilon
carbonyl carbon
* *
3
(#
,
# +
+
/
.
4witter ion
5ou may ha!e noticed that the general form for the amino acid is often drawn with the acidic
hydrogen attached to the amine group. his occurs because amine groups are basic. -o, the amino
acid has performed an acid/base reaction on itself. 6hen the amino acid is in this form it is referred
to as a 7witter ion. 6hen amino acids are in solution this is the form that they will be found.
Chirality:
$ chiral compound must contain a carbon that is bonded to four different atoms8groups. 0f you look at
the abo!e amino acids you will see that, with the exception of glycine, each structure is chiral around
the carbon with the . group. Each amino acid will come in two structural formats, called
enantiomers, an 9 and a :. 5ou were gi!en two tables of all the amino acids, the tables are only
different in the format that the amino acids are drawn. he first format is the one used to show the
chirality of the amino acid. o determine which enantiomer you ha!e you look to the location of the
hydrogen on the chiral carbon. 0f the hydrogen is on the left, then the amine group is on the right, this
is the : enantiomer. 0f the hydrogen is on the right, then the amine group is on the left, this is the 9
enantiomer. -ee the below structural diagrams;
* # (#
"
*++#
*#
,
9/alanine
* (#
"
#
*++#
*#
,
:/alanine
* # (#
"
*++#
*#
"
+#
* (#
"
#
*++#
*#
"
+#
9/serine
:/serine
he importance of chiral compounds is that their chemical reacti!ity is different. -ometimes the
difference means the compound will ha!e an ad!erse effect on a person. -ometimes the difference
means the person simple can not metaboli4e the compound. he latter is the case with amino acids.
<eaning we can consume both 9 and : amino acids, but our bodies will only metaboli4e the : form.
he en4ymes used in the metabolism of amino acids are built to fit this : form but not the 9 form.
he 9 form will pass through your body unused.
uffering:
/amino acids contain both acidic /*++# and the basic =(#
"
groups, these two functional groups
allow them to act as a buffer. >nfortunately, though, the picture is not as simple as this. 0n the
solid crystalline state the a/amino acids exist as 7witter ions, as discussed before they are formed
by the transfer of protons, #
3
from the /*++# to the =(#
"
groups. ?or /amino acids without
acidic or basic side chains these 4witter ions ha!e charged groups but are neutral o!erall. $mino
acids are found in the 7witter form e!en as solids, they form an ionic matix similar to salts.
* *
3
(#
,
# +
+
/
.
7witter ions remain when the /amino acid is dissol!ed in water at p# @. $ddition of an acid,
supplying more protons, produces ions with an o!erall positi!e charge. he amino acid forms the
below structure in an acid en!ironment.
* *
3
(#
,
# +
+
/
.
* *
3
(#
,
# +
+#
.
#
3

$ddition of a base, remo!es the acidic hydrogens, producing ions with an o!erall negati!e charge.
he amino acid forms the below structure in a basic en!ironment.
* *
3
(#
,
# +
+
/
.
* * (#
"
# +
+
/
.
+#
/
*
'
+
,
6e can describe /amino acids as amphoteric as they can react with both acid and alkali. hey
are effecti!e buffers in biological systems. he situation is more complicated in a/amino acids that
ha!e acidic or basic . groups , e.g. glu or lys.
$t !ery low p# all /amino acids exist as ions with an o!erall positi!e charge, while at high p#
they exist as ions with an o!erall negati!e charge. ?or each /amino acid there is a p# between
these extremes at which its molecules are neutral o!erall. his !alue is called the isoelectric
!oint for the /amino acid. $t its isoelectric point the /amino acid molecules will not mo!e when
placed in an electric field. he separation technique called electrophoresis relies on molecules
with different isoelectric points mo!ing at different speeds when kept at a fixed p# and placed in
an electric field.
he isoelectric point is calculated by a!eraging the pAa !alues for the carboxylic acid and the
amine group. pA
B
applies to the carboxylic acid and pA
"
applies to the amine.
+
+ -
pK pK
pI
+
=
his formula does not take into account acidic or basic side chains. 0f an acidic side chain is
present you a!erage the side chain pA
a
and pA
B
. ?or a basic side chain you a!erage the side
chain pA
a
and pA
"
.
Protein "unctions:
ype of Protein ?unction Examples
-tructure structural support collagen in tendons and cartilage
keratin in hair and nails
*ontractile muscle mo!ement actin, myosin, tubulin and kinesin proteins
ransportation mo!ement of compounds hemoglobin carries +
"
and lipoproteins carry lipids
-torage nutrient storage ferritin stores iron is spleen and li!er
casein stores proteins in milk
#ormone chemical communication insulin regulates blood sugar
En4yme *ataly4e biological reactions lactase breaks down lactose
trypsin breaks down proteins
Protection .ecogni4ed and destroy
foreign substances
immunoglobulins stimulate immune system
#eactions of Amino Acids:
o form protein, the amino acids are linked by dehydration synthesis to form peptide bonds. he
chain of amino acids is also known as a polypeptide.
Protein $tructure %y!es:
-ome proteins contain only one polypeptide chain while others, such as hemoglobin, contain se!eral
polypeptide chains all twisted together. he sequence of amino acids in each polypeptide or protein
is unique to that protein, this is call the !rimary structure. 0f e!en one amino acid in the sequence is
changed, that can potentially change the proteinCs ability to function. ?or example, sickle cell anemia
is caused by a change in only one nucleotide in the :($ sequence that causes 1ust one amino acid in
one of the hemoglobin polypeptide molecules to be different. Decause of this, the whole red blood
cell ends up being deformed and unable to carry oxygen properly.
he !rimary structure is created through the linking of amino acids. his linking is accomplished by
the formation of a peptide bond. his is a dehydration reaction. 0n other words the peptides combine
and lose a water molecule.
he peptide bonding of three alanine amino acids are shown below.
$ longer polypeptide is shown abo!e. Each peptide chain will ha!e an amine end and a carboxylic
acid end and each amino acid is referred to as a residue. -o, the ends are named, n/terminal residue
and c/terminal residue or the n/terminus and c/terminus.
he sequence of amino acids will cause the protein to ha!e areas of its shape conforming to one of ,
shapes, alpha/helical, beta/pleated sheet or wo!en 'sometimes called turns). hese are secondary
structures&
he two most common secondary structures are shown abo!e, alpha helical and beta sheet.
hese structures are created by molecular interactions between amino acids. (ormally the
interactions are hydrogen bonds. +ther interactions will form as well.
#ydrogen bonds, in the most simple explanation, from between hydrogens attached to an oxygen
or nitrogen and the lone pairs found on an oxygen or nitrogen.
:isulfide bridges form between cysteine and methionine amino acids.
-alt bridges are interactions between the ends of the 7witter ion, the (#
,
3
and the *++
/
.
#ydrophobic interactions are formed between those amino acids with hydrophobic . groups.
he abo!e picture shows an entire protein, this is called its tertiary structure. he tertiary
structure gi!es the protein its function. 0f the tertiary structure is deformed the protein will not
function. he primary structure is sequenced in a way as to form the tertiary structure. he side
chains of the amino acids cause them to interact with the other parts of the chain. hese interactions
include hydrogen bonding, hydrophobic interactions, electrostatic interactions and !an der 6aals
forces. $n egg white is all protein, when it comes out of the shell it is clear, when you cook the egg
you destroy its ertiary -tructure and the protein unfolds and becomes white, this destroys the
proteins secondary, tertiary and quaternary structures. he primary structure will normally stay intact
if the food is cooked..
-ome proteins ha!e a quaternary structure. he quaternary structure occurs in proteins composed of
more than one peptide chain. <eaning two or more proteins come together to form one large protein.
6e ha!e mentioned hemoglobin a couple of time. his large protein has a quaternary structure as it
is composed of four myoglobin subunits. Each subunit is a separate polypeptide chain.
+!erall ertiary -tructure showing;
Pink % alpha/helical area
5ellow % beta/sheet area
6hite8Dlue % wo!en or turns area
his picture is showing each of the four structure types and the order of their formation. ?irst the
primary structure is formed, as this structure forms secondary structures take shape. +nce the
protein sequence is completed the protein folds into its tertiary structure. 0f the protein has a
quantanary structure, two or more proteins will come together to complete the quantanary structure.
'estroying a Protein:
6hen a protein is destroyed it is said to be denatured. .emember that the purpose of a primary
structure is so the secondary and tertiary structures will form. *ertain conditions will cause the
protein to unfold, lea!ing only the primary structure.
heat = breaks hydrogen bonds by causing the atoms to !ibrate too radically
>E light = breaks hydrogen bonds by exciting bonding electrons
organic sol!ents = breaks hydrogen bonds
strong acids and bases = breaks hydrogen bonds and can hydroly4e the peptide bonds, breaking
the primary structure
detergents = disrupt hydrophobic interactions
hea!y metal ions = forms bonds to sulfur groups and can cause proteins to precipitate out of
solution.
(ssential and Non)(ssential Amino Acids:
$s far as your body is concerned, there are two different types of amino acids; essential and non/
essential. (on/essential amino acids are amino acids that your body can create out of other
chemicals found in your body. Essential amino acids cannot be created, and therefore the only way
to get them is through food. #ere are the different amino acids;
Non)(ssential Amino Acids:
B. $lanine 'synthesi4ed from pyru!ic acid)
". $rginine 'synthesi4ed from glutamic acid)
F
essential for infants and young children
,. $sparagine 'synthesi4ed from aspartic acid)
G. $spartic $cid 'synthesi4ed from oxaloacetic acid)
5. *ysteine 'synthesi4ed from homocysteine, which comes from methionine)
H. 2lutamic $cid 'synthesi4ed from oxoglutaric acid)
@. 2lutamine 'synthesi4ed from glutamic acid)
I. 2lycine 'synthesi4ed from serine and threonine)
J. Proline 'synthesi4ed from glutamic acid)
B0. -erine 'synthesi4ed from glucose)
BB. ryosine 'synthesi4ed from phenylalanine)
* * #
#
#
+
*
+
+#
pyru!ic acid
* * (#
"
# +
+#
*#
"
*#
"
* +
+
#
glutamic acid aspartic acid
* * (#
"
# +
+#
*#
"
* +
+
#
* * *
#
#
+
*
+
+# #+
+
oxaloacetic acid
* * *
#
#
+
*
+
+# *
#
# +
#+
oxoglutaric acid
+
*#
"
+#
#
#
+#
#+
# +#
#
#+
#
alpha /:/glucose
* * (#
"
# +
+#
*#
"
phenylalanine
* * (#
"
# +
+#
*#
"
+#
serine
* * (#
"
# +
+#
*
*
#
# #
# +#
threonine

* * (#
"
# +
+#
*#
"
*#
"
-
*#
,
methionine

homocysteine
* * (#
"
# +
+#
*#
"
*#
"
-#
(ssential Amino Acids:
B. #istidine
". 0soleucine
,. 9eucine
G. 9ysine
5. <ethionine
H. Phenylalanine
@. hreonine
I. ryptophan
J. Ealine
Protein Nutrition:
Protein in our diets comes from both animal and !egetable sources. <ost animal sources 'meat, milk,
eggs) pro!ide whatKs called &complete protein,& meaning that they contain all of the essential amino
acids. Eegetable sources usually are low on or missing certain essential amino acids. ?or example,
rice is low in isoleucine and lysine. #owe!er, different !egetable sources are deficient in different
amino acids, and by combining different foods you can get all of the essential amino acids throughout
the course of the day. -ome !egetable sources contain quite a bit of protein // things like nuts, beans,
soybeans, etc. are all high in protein. Dy combining them you can get complete co!erage of all
essential amino acids.
he digesti!e system breaks all proteins down into their amino acids so that they can enter the
bloodstream. *ells then use the amino acids as building blocks.
?rom this discussion you can see that your body cannot sur!i!e strictly on carbohydrates. 5ou must
ha!e protein. $ccording to this article, the .:$ '.ecommended :aily $llowance) for protein is 0.,H
grams of protein per pound of body weight. -o, a B50/pound person needs 5G grams of protein per
day.
$thletes will need more in their diets. <any studies ha!e recommended protein le!els of B gram of
protein per kilogram of body weight per day. 6hich is near three times that of a non/acti!e person.
0f you would like to read some good sports nutrition texts, try &he $thleteKs Aitchen& by (ancy *lark
<- .: or &-ports (utrition& by :an Denardot Ph.:., .:. -ports nutrition for children, try &Play #ard
Eat .ight& by :ebbi -owell Lennings <- .: and -u4anne (elson -teen :.-c. .:.
must be consumed
he nutritional facts picture is the (utritional ?acts label from a
package of bacon. 5ou can see that a ser!ing of this bacon has G
grams of protein. here are J ser!ings in this package gi!ing a total
of ,H grams of protein. $n I ounce glass of milk contains about I
grams of protein. $ slice of whole grain bread may contain " or ,
grams of protein. 5ou can see that it is not that hard to meet the
.:$ for protein with a normal diet. $ fried egg will ha!e about I
grams of protein. -o, a typical breakfast may consist of " fried
eggs, " pieces of toast and a glass of milk gi!ing you about ,0
grams of protein 1ust for breakfast. $ B50 lb person is well on their
way to meeting their .:$ of 5G grams of protein.
Analy*ing Amino Acids:
(lectro!horesis:
$bo!e are pictures of gel electrophoresis. he protein is denatured so that it loses all secondary
and tertiary structure. his means you ha!e the protein as a string of amino acids. 0t is because
of this string/like form that you can separate proteins based on their molecular weight alone. $
protein standard solution, a mixture of proteins of known molecular masses, is loaded into lane
spot MB. he protein samples that are your unknowns are loaded into other ad1acent lanes M" N
M,.
0n electrophoresis an electric potential difference is applied across a plate of gel. <olecules
separate on the gel since they mo!e at speeds that depend on their si4e. -maller proteins mo!e
at a faster rate than larger proteins. 6hen the protein bands ha!e migrated down the gel one can
compare the molecular weights of the unknown proteins to the standard protein molecular
masses.
%est #eagents for Amino Acids:
Oanthoproteic est;
positi!e test for ben4ene rings which ha!e amino or hydroxyl groups, such as that present in
tryptophan and tyrosine
addition of concentrated #(+
,
.
gi!es yellow color and is intensified to orange/yellow by the addition of a base
*ysteine est;
positi!e test for cysteine
addition of cyanide salt to reduce disulfide bonds
addition of nitroprusside to from a colored complex with sulfhydryl groups
gi!es a pink to purple color intensity increases with concentration of =-# groups
if no nitroprusside is used a black ppt will indicate positi!e test
nitroprusside
Diuret est;
positi!e test for peptide bonds
Diuret .eagent is made of sodium hydroxide and copper sulfate
blue reagent turns !iolet in the presence of proteins
pink color persists with short/chain polypeptides
color intensity !aries with concentration of peptides
(inhydrin est;
positi!e test for amino acids, not peptides
all amino acids gi!e blue
except proline which gi!es a yellow color
-anger .eagent;
.eagent for the determination of the (/terminal amino acid in a peptide.
0n the first step the amino group is coupled to B/fluoro/",G/dinitiroben4ene 'by a nucleophilic
aromatic substitution).
hen the peptide is hydrolytically clea!ed. 0f the hydrolysis is mild enough 'which can be quite
annoying), then the whole peptide can be degradated !ia this reaction.
$fter the clea!age the dinitrophenyl residue is still connected to the (/terminal amino acid. hat
can easily be separated and analy4ed by e.g. chromatography
Edman :egradation;
:egradation of the (/terminal amino acid of a peptide.
hen the amino acid can be identified e.g. with chromatographic methods or melting point.
+ (ssential Amino Acids: "unction, 'eficiencies and (xcesses
H-$%-'-N(
.ain "unctions:
?ound in high concentrations in hemoglobin.
>seful in treating anemia due to relationship to hemoglobin.
#as been used to treat rheumatoid arthritis.
Precursor to histamine.
$ssociated with allergic response and has been used to treat allergy.
$ssists in maintaining proper blood p#.
Histidine (xcess -n:
Pregnancy
Histidine 'eficiency $een -n:
.heumatoid arthritis
$nemia
:ysbiosis '0mbalance of intestinal bacterial flora).
Note:
#igh #istidine le!els are associated with low 4inc le!els. 9ow #istidine le!els are associated with high
4inc le!els. hus, abnormal #istidine le!els are an indicator that 4inc le!els should be tested.
-$O/(0C-N(
.ain "unctions:
+ne of the , ma1or Dranched/*hain $mino $cids 'D*$$), all of which are in!ol!ed with muscle
strength, endurance, and muscle stamina.
<uscle tissue uses 0soleucine as an energy source.
.equired in the formation of hemoglobin.
D*$$ le!els are significantly decreased by insulin. ranslation; #igh dietary sugar or glucose intake
causes release of insulin, which, in turn, causes a drop in D*$$ le!els. herefore, right before
exercise, it is not wise to ingest foods high in glucose or other sugars, as the D*$$Ks, including
0soleucine will not be readily a!ailable to muscles.
-soleucine (xcess $een -n:
:iabetes <ellitus with ketotic hypoglycemia
-soleucine 'eficiency $een -n:
+besity
#yperinsulinemia
Panic :isorder
*hronic ?atigue -yndrome '(ote; :eficiencies in D*$$ in *?-, 26-, ?< are associated with
muscle weakness, fatigue, and post/exertional exhaustion).
$cute hunger
Awashiorkor 'star!ation)
/(0C-N(
.ain "unctions:
$s one of the , branched/chain amino acids 'the other " being 0soleucine and Ealine), 9eucine has all
of the properties discussed with 0soleucine, as it pertains specifically to the branched/chain amino
acid functions.
Potent stimulator of insulin.
#elps with bone healing.
#elps promote skin healing.
<odulates release of Enkephalins, which are natural pain/reducers.
/eucine (xcess $een -n:
Aetosis
/eucine 'eficiency $een -n:
#yperinsulinemia
:epression
*hronic ?atigue -yndrome '(ote; :eficiencies in D*$$ in *?-, 26-, ?< are associated with
muscle weakness, fatigue, and post/exertional exhaustion).
$cute hunger
Awashiorkor 'star!ation)
Eitamin D/B" deficiency in pernicious anemia
/1$-N(
.ain "unctions:
0nhibits !iral growth and, as a result, is used in the treatment of #erpes -implex, as well as the
!iruses associated with *hronic ?atigue -yndrome, such as; Epstein/Darr Eirus, *yto<egalo Eirus,
and ##EH.
9/*arnitine is formed from 9ysine and Eitamin *.
#elps form collagen, the connecti!e tissue present in bones, ligaments, tendons, and 1oints.
$ssists in the absorption of calcium.
Essential for children, as it is critical for bone formation.
0n!ol!ed in hormone production.
9owers serum triglyceride le!els.
/ysine (xcess $een -n:
Excess of ammonia in the blood
/ysine 'eficiency $een -n:
#erpes
Epstein/Darr Eirus
*hronic ?atigue -yndrome
$0:-
$nemia
#air loss
6eight loss
0rritability
.(%H-ON-N(
.ain "unctions:
$ssists in breakdown of fats.
Precursor of the amino acids *ysteine and aurine.
#elps reduce blood cholesterol le!els.
$ntioxidant.
$ssists in the remo!al of toxic wastes from the li!er.
+ne of the sulfur/containing aminos 'the others being *ysteine and the minor amino acid, aurine).
he sulfur/containing amino acids act as anti/oxidants which neutrali4e free radicals.
#elps pre!ent disorder of hair, skin, and nails due to sulfur and anti/oxidant acti!ity.
Precursor to *arnitine, <elatonin 'the natural sleep aid) and *holine 'part of the neurotransmitter,
$cetylcholine).
0n!ol!ed in the breakdown of Epinephrine, #istamine, and (icotinic $cid.
.equired for synthesis of .($ and :($.
(atural chelating agent for hea!y metals, such as lead and mercury.
.ethionine (xcess $een -n:
-e!ere li!er disease
.ethionine 'eficiency $een -n;
*hemical Exposure
<ultiple *hemical -ensiti!ity '<*-)
Eegan Eegetarians
PH(N1/A/AN-N(
.ain "unctions:
Precursor to yrosine, which, in turn, is the precursor to the neurotransmitters; :opamine and the
excitatory neurotransmitters (orepinephrine and Epinephrine.
Precursor to the hormone, hyroxin.
Enhances mood, clarity of thought, concentration, and memory.
-uppresses appetite.
<a1or part of collagen formation.
6hile the 9/form of all of the other amino acids is the one that is beneficial to people, the
: and :9 forms of Phenylalanine ha!e been useful in treating pain.
:9/Phenylalanine is useful in reducing arthritic pain.
Powerful anti/depressant.
>sed in the treatment of ParkinsonKs :isease.
Phenylalanine (xcessi2e $een -n:
Pregnancy
pigmented melanoma
PA> 'phenylketonuria)
panic disorder8anxiety attacks.
Phenylalanine 'eficiency $een -n:
:epression
+besity
*ancer
$0:-
ParkinsonKs :isease
(ote;
Phenylalanine should be a!oided if you suffer from #igh blood pressure, as it has hypertensi!e.
%H#(ON-N(
.ain "unctions:
.equired for formation of collagen.
#elps pre!ent fatty deposits in the li!er.
$ids in production of antibodies.
*an be con!erted to 2lycine 'a neurotransmitter) in the central ner!ous system.
$cts as detoxifier.
(eeded by the 20 'gastrointestinal) tract for normal functioning.
Pro!ides symptomatic relief in $9- '$myotrophic 9ateral -clerosis, 9ou 2ehrigKs :isease).
0n laboratory experiments with animals, hreonine increases thymus weight.
hreonine is often low in depressed patients. 0n that group of patients, hreonine is helpful in treating
the depression.
%hreonine (xcess $een -n:
$lcohol ingestion
hose treated with sedati!e anti/con!ulsing medication 'animal studies)
Eitamin DH deficiency
Pregnancy
9i!er cirrhosis
%hreonine 'eficiency $een -n:
:epression
$0:-
<uscle -pasticity
$9- '$myotrophic 9ateral -clerosis)
Eegetarianism
Epilepsy
%#1P%OPHAN
.ain "unctions:
Precursor to the key neurotransmitter, serotonin, which exerts a calming effect.
Effecti!e sleep aid, due to con!ersion to serotonin.
.educes anxiety.
Effecti!e in some forms of depression.
reatment for migraine headaches.
-timulates growth hormone.
$long with 9ysine, *arnitine, and aurine is effecti!e in lowering cholesterol le!els.
*an be con!erted into niacin 'Eitamin D,).
9owers risk of arterial spasms.
he only plasma amino acid that is bound to protein.
ryptophan must compete with 5 other amino acids to pass through the blood/brain barrier and enter
the brain. hose 5 are; tyrosine, phenylalanine, leucine, isoleucine, and !aline and are called 9arge
(eutral $mino $cids '9($$).
.equires pyridoxal/5/phosphate 'P5P) a form of !itamin DH to be con!erted into serotonin. P5P
deficiency will lower serotonin le!els, e!en if ryptophan le!els are normal.
%ry!to!han (xcess $een -n:
0ncreased intake of salicylates 'aspirin).
0ncreased blood le!els of free fatty acids.
-leep depri!ation.
(iacin intake.
%ry!to!han 'eficiency $een -n:
:epression
0nsomnia
*hronic ?atigue -yndrome
$9-
?:$ ban of ryptophan
Note:
-imultaneous treatment with ryptophan and Pro4ac 'and other --.0 anti/depressants, such as Paxil
and 7oloft) can produce an irre!ersible brain disorder called -erotonin -yndrome. his treatment
combination is to be a!oided.
-tandard $<$, $P$ '$merican Psychiatric $ssociation), ?:$, and pharmaceutical industry position
has been that ryptophan is not an effecti!e treatment of serotonin/depletion depressions, when
compared to Pro4ac and other --.0Ks.
*linical experience has shown that some people respond well to Pro4ac while others respond well to
ryptophan in treating serotonin/depleted depressions. 6hen the ?:$ banned ryptophan,
thousands of people who only had a positi!e response to ryptophan 'and not to Pro4ac)
decompensated psychologically and ne!er reco!ered.
ryptophan is again a!ailable, but only through prescription and compounding pharmacies.
3A/-N(
.ain "unctions:
+ne of the , ma1or Dranched/*hain $mino $cids 'D*$$) . . .the other " being leucine and
isoleucine . . . all of which are in!ol!ed with muscle strength, endurance, and muscle stamina.
D*$$ le!els are significantly decreased by insulin. #igh dietary sugar or glucose intake causes
release of insulin, which, in turn, causes a drop in D*$$ le!els.
*ompetes with yrosine and ryptophan in crossing the blood/brain barrier. he higher the Ealine
le!el, the lower the brain le!els of yrosine and ryptophan. +ne of the implications of this
competition is that yrosine and ryptophan nutritional supplements need to be taken at least an hour
before or after meals or supplements that are high in branched chain amino acids.
$cti!ely absorbed and used directly by muscle as an energy source.
(ot processed by the li!er before entering the blood stream.
$ny acute physical stress 'including surgery, sepsis, fe!er, trauma, star!ation) requires higher
amounts of Ealine, 9eucine and 0soleucine that any of the other amino acids.
:uring period of Ealine deficiency, all of the other amino acids 'and protein) are less well absorbed by
the 20 tract.
3aline (xcess $een -n:
Aetotic #ypoglycemia
Eisual and tactile hallucinations
3aline 'eficiency $een -n:
Awashiorkor
#unger
+besity
(eurological deficit
Ele!ated insulin le!els