AMINO ACIDS

Amino acids are the monomeric units of proteins. Although about 300 amino acids occur in nature, only 20 of them are seen in proteins.

General structure fro amino acids

Has an Amino group (-NH2) and a carbo ylic group (-!""H) both of them bonded to an alpha carbon atom. #n addition they contain a side chain (-$) %he side chain &aries from one amino acid to other.

!lassification of aminoacids based on structure

#. Aliphatic amino acids

###. Aromatic amino acids #'. Heterocyclic amino acids '. #mino acids

I. Aliphatic amino acids Simple amino acids (. )lycine()ly) *)+

2.

Alanine(Ala) *A+

Aliphatic amino acids

Branched chain amino acids

3. 'aline ('al) *'+

,. -eucine (-eu)

*-+

.. #soleucine (#le) *#+

Aliphatic amino acids

Branched chain amino acids

Aliphatic amino acids

Hydroxy amino acids /. 0erine (0er) *0+

1. %hreonine (%hr)*%+

2. 3ethionine (3et)

*3+

Amino acids containin 4. !ysteine 2. 3ethionine

Sulphur *!+ *3+

(!ys) (3et)

Aliphatic amino acids

Mono amino dicar!oxylic amino acids (0. Aspartic acid ((. )lutamic acid (Asp) ()lu) *5+ *6+

Acid amides (2. Asparagine (3. )lutamine (Asn) ()ln) *7+ *N+

Aliphatic amino acids

Di!asic mono car!oxylic amino acids (,. -ysine (-ys) *8+

(.. Arginine

(Arg)*$+

II. Aromatic amino acids (/. 9henyl alanine (9he) *:+

(1. %yrosine

(%yr) *;+

III. Heterocyclic amino acids (4. %ryptophan (%rp) *<+

(2. Histidine (His) *H+ I". Imino acids 20. 9roline (9ro) *9+

!lassification based on 9olarity

Non polar 9olar =ith positi&e charged grous 9olar =ith negati&ely charged gropd 9olar =ith No charge

Non-polar amino acids

Polar, non-charged amino acids

Negatively-charged amino acids

Positively-charged amino acids

!lassification based on the reaction of side chain groups

Acidic# Asp$ Glu Basic# %ys - 6psilon amino group Ar - )uanido gp His - #mida>ole gp Neutral# Gly$ Ala$ "al$ %eu$ Ile$ Ser$ &hr$ Cys$ Met$ Asn$ Gln$ 'he$ &yr$ &rp$ 'ro.

Classification of Amino acids

Dependin on Meta!olic fate

)lucogenic

Gly$ Ala$ "al$ Ser$ &hr$ Cys$ Met$ Asp$ Glu$ Asn$ Gln$ Ar $ His$ 'ro

8etogenic
%eu

?oth )lucogenic and 8etogenic

%ys$ Ile$ 'he$ &yr$ &rp

!lassification based on nutritional re@uirement

?acteria can synthesi>e all the 20 amino acids. ?ut humans cannot synthesi>e all the 20 amino acids due to lacA of en>ymes. 0o those amino acids =hich cannot be synthesi>ed in the body has to be supplied in the diet. %hese are called (ssential Amino acids %hose =hich can be synthesi>ed in the body are called Nonessential amino acids

!lassification based on nutritional re@uirement

(ssential amino acids )Indispensa!le* )+* "al 'he Ile %eu &rp %ys &hr Met
Very Few Indians Love Watching Live Tennis Matches

Semi essential amino acids# !an be synthesi>ed in the body but has to be supplied during gro=thAr $ His Nonessential amino acids )Dispensa!le*),-* Gly$ Ala$ Ser$ &hr$ Cys$ Asp$ Glu$ Asn$ Gln$ 'ro

3odified amino acids in proteins (5eri&ed amino acids)

All the 20 AAs ha&e a codon in the genetic code B specific t$NAs and they get incorporated to polypeptides by translation. !ertain of these amino acids after incorporation to proteins are modified. (9ost translational modifications)

3odified amino acids in proteins (5eri&ed amino acids)

,../Hydroxy %ysine 0.Hydroxy 'roline Hydro y proline and Hydro y lysine seen in !ollagen. 1.N/ Methyl %ysine C 0een in 3yosin ,. N/ 2ormyl Methionine (?acteria)

3odified amino acids in proteins (5eri&ed amino acids)

.. Gamma car!oxy lutamic acid/ !lotting factors are acti&ated by gamma carbo ylation. $e@uires 'it 8 as coen>yme 3. Cystine - #f 2 cysteine residues are adDacent they form disulphide bonds to form !ystine.

"ther ?iologically important amino acids

0ome amino acids are not seen in proteins but ha&e biological importance. %hey are formed during metabolism. 6 amples Homocysteine Homoserine "rnithine !itrulline

?iologically important Non- alpha amino acids

Amino acids found in proteins are alpha amino acids. ?ut there are certain non alpha amino acids =hich perform important functions in metabolism. 6 amples (.?eta Alanine 2.%aurine 3.)amma amino butyric acid ()A?A)

'roperties of amino acids#

%hey are colorless, crystalline substances more soluble in =ater &aste# )lycine, alanine, 'aline, 0erine, %ryptophan, Histidine and 9roline are s=eet in taste. -eucine is tasteless. #soleucine and Arginine are bitter in taste

 Meltin point# All amino acids ha&e high melting points. #.e. more than 200o! Solu!ility# All amino acids are soluble in =ater and alcohol. ?ut insoluble in non polar sol&ents 6.g. ben>ene

0tereoisomerism
A molecule =ith non super impossible mirror images are Ano=n as chiral. !hiral molecules possess a Echiral centreF usually a carbon atom. A chiral carbon atom is one =hich all its four different &alencies are satisfied by four different atoms or group. All amino acids e cept glycine has at least one chiral carbon atom )lycine is achiral.

 5ue to the presence of chiral carbon atom aminoacids e cept )lycine e hibit stereoisomerism (5- isomerism) %he t=o stereo isomers of each amino acid are designated as -- and 5-amino acids on the basis of their similarity to the glyceraldehyde standard. <hen the NH2 group of an amino acid is oriented to=ard right it is the 5 form and if NH2 group is oriented left it is - isomer. %he amino acids that occur in proteins are all of the form. 5 amino acids occur in nature, most often in bacterial cell =alls and in some antibiotics.

 Ampholyte nature# All amino acids contain ioni>able groups -!""H and -NH2. 5epending on the pH of the medium amino acids can e ist as Anions or !ations. #n acidic solutions they remain as cations and in alAaline solutions they remain as anions At a particular pH they carry both positi&e and negati&e charge and Ano=n as 45itter ion. 0o their net charge =ill be Gero

 %he pH at =hich a compound e ists as G=itter ion is Ano=n as isoelectric pH %he solubility =ill be minimum at isoelctric pH %here is no mobility in electric field at this pH

96%#56 ?"N5
Amino acids in protein are held together by peptide bond 9eptide bond is formed bet=een the alpha amino group of an aminoacid and the carbo ylic group of another aminoacid. <hent=o amino acids are linAed by a peptide bond it is Ano=n as dipeptide <hen three amino acids are linAed by t=o peptide bond it is Ano=n as tripeptide <hen moret than ten amino acids are linAed by peptide bond then it is Ano=n as polypeptide

Charecteristics of peptide !ond#

9eptide bond is partially double bond in character #t is planar. %he distance of peptide bond is (.32 Ao. :ormed bet=een amino group og one aminoacid and carbo ylic group of another amino acid