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Proteins: An Overview

Proteins are made up of chains of amino acids and play essential structural and functional roles in the body. There are 20 standard amino acids that make up proteins and each has a unique side chain that determines its properties. Amino acids can be classified based on characteristics of their side chains such as being polar, nonpolar, acidic, or basic, which influence how they interact and allow proteins to fold into complex 3D shapes to perform their functions.
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0% found this document useful (0 votes)
56 views6 pages

Proteins: An Overview

Proteins are made up of chains of amino acids and play essential structural and functional roles in the body. There are 20 standard amino acids that make up proteins and each has a unique side chain that determines its properties. Amino acids can be classified based on characteristics of their side chains such as being polar, nonpolar, acidic, or basic, which influence how they interact and allow proteins to fold into complex 3D shapes to perform their functions.
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PROTEINS

D and L:

 Absolute
Proteins are not alien to you configuration
Hair and nails - made up of the protein alpha keratin  Based on
glyceraldehyde
Muscle proteins called actin and myosin enable body  Does not indicate
movement. the direction by
Blood – haemoglobin protein carries O2 to every parts of which the molecule
your body rotate plane
polarized light
Proteins: an overview

 Major constituent of most cells. (>50% dry weight)


 Very diverse molecules.
 Define what an organism is, what it looks like, how
it behaves, etc. (responsible for most phenotype).
 made up of the 20 standard amino acids

Basic Amino Acid Structure

Composed of:
Amino Acid Classification
 central carbon
 carboxylic acid  Alkyl/Aliphatic (Nonpolar)
group  Aromatic
 amino group  Sulfur-containing
 R group:  Polar, uncharged
o variable  Basic
o distinguishes amino acids and their  Acidic
properties Alkyl Amino Acids
Central carbon Alanine (Ala, A) - methyl-group
 α-carbon
 tetrahedral geometry
surrounded by 4
 different groups
 Chiral!
 enantiomers exist
 only L-isomer occurs
naturally

Leucine (Leu, L)
Glycine (Gly, G) - only non-chiral amino acid

Isoleucine (Ile, I) - 2 chiral carbons


Sulfur Containing Amino Acids

Methionine (Met, M) – very hydrophobic

Proline (Pro, P) - cyclic “imino acid”

Cysteine (Cys, C) – sulfur in form of sulfhydryl, important in


disulfide linkages

Valine (Val, V) - think V!


Acids

 contain carboxyl groups (weaker acids than α-


carboxyl-group)
 negatively charged at physiological pH (therefore –
ate not –ic acids)

Aspartate (Asp, D)

Bases

 hydrophilic nitrogenous bases


 positively charged at physiological pH

Histidine (His, H) - imidazole ring protonated/ionized

Glutamate (Glu, E)

Lysine (Lys, K) - diamino acid, protonated at pH 7.0


Tyrosine (Tyr, Y) - OH ionisable

Arginine (Arg, R) - guanidinium ion always protonated,


most basic amino acid

Tryptophan (Trp, W) - bicyclic indole ring

Aromatic Amino Acids


Alcohols
 All very hydrophobic
 All contain aromatic group  Polar side groups, hydrophilic in nature, can form
 Absorb UV at 280 nm hydrogen bonds
Phenylalanine (Phe, F) Serine (Ser, S) - looks like Ala w/ -OH
Threonine (Thr, T) - 2 chiral carbons Arginine Arg R (“aRginine”)
Asparagine Asn N (contains N)
Aspartate Asp D (“asparDic”)
Glutamate Glu E (“glutEmate”)
Glutamine Gln Q (“Q-tamine”)
Phenylalanine Phe F(“Fenylalanine”)
Tyrosine Tyr Y (“tYrosine”)

Protonic Equilibria of Amino Acids

 Exhibit acid-base properties due to their α-COOH


and α-NH2 groups
 Additional acidic/basic group may be present in the
Amides side chain
 Polar side groups, hydrophilic in nature, can form  pKas of amino acids are known
hydrogen bonds o α-COOH: pKa≈ 2
o α-NH3: pKa ≈ 9
Asparagine (Asn, N) - amide of D  Have characteristic titration curves

Glutamine (Gln, Q) - amide of E


Titration Curve of Glycine

Abbreviations and Symbols for Amino Acids

Similar Sounding Names


Amino Acids as Buffers

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