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Amino Acids

Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up protein monomers. Amino acids contain an amino group, a carboxyl group, and a side chain that gives each amino acid its unique chemical properties. The side chains allow for different interactions like hydrophobic interactions between non-polar amino acids and ionic interactions between charged amino acids. Proline has a secondary amine group that makes it more stable but can disrupt protein structures. Cysteine can form disulfide bridges. These interactions are important for determining protein structure and function.

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12 views

Amino Acids

Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up protein monomers. Amino acids contain an amino group, a carboxyl group, and a side chain that gives each amino acid its unique chemical properties. The side chains allow for different interactions like hydrophobic interactions between non-polar amino acids and ionic interactions between charged amino acids. Proline has a secondary amine group that makes it more stable but can disrupt protein structures. Cysteine can form disulfide bridges. These interactions are important for determining protein structure and function.

Uploaded by

ayesha jalal234
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Amino Acids

Date Created @November 9, 2023 6:45 PM

Status Done 🙌
AA: monomeric unit of a protein
300 naturally occurring
20 constitute of monomers units of proteins

NON-ESSENTIAL ( already produced by the


ESSENTIAL AA ( supplied by diet) 9
body) 11

Histidine Isoleucine Leucine Lysine Alanine Arginine Asparagine Aspartic acid


Methionine Phenylalanine Threonine Cysteine Glutamic acid Glutamine Glycine Proline
Tryptophan Valine Serine Tyrosine

Sulphur containing Imino Acid with secondary amine NH

Methionine + Cysteine PROLINE

Side chain, or R group confers the chemical signature to the amino acid—> chem
properties.

Alpha carbon is a chiral centre (- amine + COOH R group+ H

resulting in non-superimposable mirror images known as


enantiomers.

Alpha carbon: directly bonded to the functional group in an organic compound

Amino Acids 1
✓ All molecules with a chiral center are optically active
✓ That is these molecules rotate plane polarized light

IMINO (PROLINE) VS AMINO


IMINO ACID: PROLINE contain both an amide and a carboxyl group, bonded to
the alpha carbon molecule. Difference in nitrogen bonding (has a secondary
amine group R-NH) when bonded
whereas amino acids contain a primary amine group NH2—ALWAYS CYCLIC AND
MORE STABLE (NO FREE H)

PROLINE—> GLUTAMATE=INTERCONVERTIBLE —- RIGID N HELIX BREAKER—


>DISRUPTS 2nd structures (Alpha helices)

Amino Acids 2
Cysteine (oxidised to ——>cystine) Cystine
Has a thiol (SH) group Dimer of cysteine (S)

Amino Acids 3
NON POLAR AA AND HYDROPHOBIC INTERACTIONS:

"VAIL MP":

1. V: Valine

2. A: Alanine

3. I: Isoleucine

4. L: Leucine

5. M: Methionine

6. P: Proline

✓ When one places two hydrophobic amino acids close by, they will
interact with each other to stay away from water.
✓ This kind of interaction is defined as hydrophobic interaction between
amino acid (EG-Isoleucine + leucine form hydrophobic interactions)

POLAR - IONIC INTERACTIONS

Amino Acids 4
STTaY CHaRGED (without the As)

CHARGED POLAR

+ Basic or - acidic charge so forms AA forms Hydrogen Bonding with water due to
electrostatic interactions/ionic bonds unequal distribution of electrons

Charged ion Side chain has electronegative atoms

BOTH Hydrophillic

Aspartic and Glutamic acid HAL-Histidine+ Serine, Threonine, Tyrosine, Cysteine,


Arginine +Lysine Asparagine, Glutamine.

1. S: Serine

2. T: Threonine

3. T: Tyrosine

4. Y: Tyrosine

5. C: Cysteine

6. H: Histidine

7. R: Arginine

8. E: Glutamic Acid (aspartate and glutamate are negatively charged) ACIDIC

Amino Acids 5
9. D: Asparagine (asparagine and glutamine are polar but uncharged)

HAL- His +Arg + Lys-Basic charged

AROMATIC (PTT) - PI-PI Interactions/ Stacking


Interaction- NON COVALENT+ATTRACTIVE
INTERACTIONS

Amino Acids 6
Attraction is due to dipole-dipole forces between 2 polar molecules (water is more
polar than HF)

Repulsion is due to London dispersion forces —> exists between all molecules—
temporary uneven distribution of electrons
Alignment of positive
electrostatic potential on one
ring with negative electrostatic
potential on another ring
forms an interaction

Pi +/- with PTT

Pi-Cation Pi-Anion

non-covalent interaction between a cation,


non-covalent interaction between a anion, or a
or a positively charged portion of a
negatively charged portion of a molecule, and the
molecule, and the face of an aromatic π
face of an aromatic π system.
system.

pi-cation interactions with positively


not with acidic ones generally—→ mainly with
charged groups, such as those in the side
nucleic acids(phosphate grp)+membrane
chains of lysine or arginine (BASIC SO
phospholipids+ligands+carboxylate ions
POSITIVE).

in LACTATE OXIDASE (lactate to pyruvate)—→There is a Tyr-mediated hydrogen


bond formation

Amino Acids 7
COLLAGEN STRUCTURE And Hydroxy-OH derivatives of
PROLINE + LYCINE

GLUTAMATE——>CARBOXYLATION—>CARBOXYGLUTAMATE—
→High affinity for Ca 2+

Amino Acids 8
4 LYSINE—→ DESMOSINE—→Presence in ELASTIN

Amino Acids 9

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