Amino Acids & Proteins

Amino Acids &Amino Acids & Proteins Proteins

Ghollam-Reza Moshtaghi-KashanianGhollam-Reza Moshtaghi-KashanianBiochemistry DepartmentBiochemistry Department

Medical SchoolMedical SchoolKerman University of Medical sciencesKerman University of Medical sciences

IntroductionIntroduction

Most biologically important macromolecules are Most biologically important macromolecules are polymers, called biopolymers.polymers, called biopolymers.

Biopolymers fall into three classes:Biopolymers fall into three classes:– polysaccharides (carbohydrates), polysaccharides (carbohydrates), – proteins,proteins,– nucleic acids.nucleic acids.

ProteinsProteinsAmino AcidsAmino AcidsProteins are large molecules present in all cells.Proteins are large molecules present in all cells.

They are made up of They are made up of -amino acids.-amino acids.

There are two forms of an amino acid: one that is There are two forms of an amino acid: one that is neutral (with -NHneutral (with -NH22 and -COOH groups) and one and -COOH groups) and one that is zwitterionic (with -NHthat is zwitterionic (with -NH33

++ and -COO and -COO-- groups). groups).

A zwitterion has both positive and negative charge A zwitterion has both positive and negative charge in one molecule.in one molecule.

There are about 20 amino acids found in most There are about 20 amino acids found in most proteins. proteins.

Structure and Properties of Amino-acids, Structure and Properties of Amino-acids, Protein Primary StructureProtein Primary Structure

-Proteins are polymers made out by the condensation of amino-acids

-strings of amino-acids are called polypeptide chains.

-There are 20 different chemical kinds of natural amino-acids plus some

special variants.

-Each protein has a specific sequence of amino-acids (primary structure), which is determined by the DNA sequence of the gene encoding for the protein.


-Proteins with the same function from different organisms have similar primary structures

-Amino-acid sequence determines the 3-D structure in which the protein folds and its biological function.

-Proteins can have very different sizes (from 30 to ~ 100,000 residues)

-The basic module in primary sequence is the protein domain


-some proteins are monodomain others are multidomain in one chain

-some proteins are composed by more than one polypeptide chain

-Proteins can be characterized spectroscopically-Proteins can be isolated and purified based on

their differential chemical and physical properties

Amino AcidsAmino Acids

FundamentalsFundamentals

While their name implies that amino acids are While their name implies that amino acids are compounds that contain an —NHcompounds that contain an —NH2 2 group and a group and a —CO—CO22H group, these groups are actually H group, these groups are actually present as —NHpresent as —NH33

++ and —CO and —CO22–– respectively. respectively.

They are classified as They are classified as , , , , , , etcetc. amino acids . amino acids according the carbon that bears the nitrogen.according the carbon that bears the nitrogen.

Amino AcidsAmino Acids NNHH33

++

CCOO22––

an an -amino acid that is an-amino acid that is anintermediate in the biosynthesisintermediate in the biosynthesisof ethyleneof ethylene

++HH33NNCHCH22CHCH22CCOO22

––a a -amino acid that is one of-amino acid that is one ofthe structural units present inthe structural units present incoenzyme Acoenzyme A

++HH33NNCHCH22CHCH22CHCH22CCOO22

–– a a -amino acid involved in-amino acid involved inthe transmission of nervethe transmission of nerveimpulsesimpulses

The 20 (22) Key Amino AcidsThe 20 (22) Key Amino Acids

More than 700 amino acids occur naturally, but More than 700 amino acids occur naturally, but 20 (22?)of them are especially important.20 (22?)of them are especially important.

These 22 amino acids are the building blocks of These 22 amino acids are the building blocks of proteins. All are proteins. All are -amino acids.-amino acids.

They differ in respect to the group attached to They differ in respect to the group attached to the the carbon. carbon.


CC CC

OO

OO––

RR

HH

HH33NN++

The amino acids obtained by hydrolysis of The amino acids obtained by hydrolysis of proteins differ in respect to proteins differ in respect to R R (the side chain).(the side chain).

The properties of the amino acid vary as the The properties of the amino acid vary as the structure of structure of RR varies. varies.


CC CC

OO

OO––

HH

HH

HH33NN++

Glycine is the simplest amino acid. It is the only Glycine is the simplest amino acid. It is the only one in the table that is achiral.one in the table that is achiral.

In all of the other amino acids in the table the In all of the other amino acids in the table the carbon is a stereogenic center.carbon is a stereogenic center.

GlycineGlycine

(Gly or G)(Gly or G)

Glycine Glycine (Gly or G)(Gly or G)


CC CC

OO

OO––

CHCH33

HH

HH33NN++

AlanineAlanine(Ala or A)(Ala or A)

Alanine Alanine (Ala or A)(Ala or A)


CC CC

OO

OO––

CH(CHCH(CH33))22

HH

HH33NN++

ValineValine(Val or V)(Val or V)

Valine Valine (Val or V)(Val or V)


CC CC

OO

OO––

CHCH22CH(CHCH(CH33))22

HH

HH33NN++

LeucineLeucine(Leu or L)(Leu or L)

Leucine Leucine (Leu or L)(Leu or L)


CC CC

OO

OO––

CHCH33CHCHCHCH22CHCH33

HH

HH33NN++

IsoleucineIsoleucine(Ile or I)(Ile or I)

IsoleucineIsoleucine (Ile or I)(Ile or I)


CC CC

OO

OO––

CHCH22OHOH

HH

HH33NN++

SerineSerine(Ser or S)(Ser or S)

Serine Serine (Ser or S)(Ser or S)


CC CC

OO

OO––

CHCH33CHOHCHOH

HH

HH33NN++

ThreonineThreonine(Thr or T)(Thr or T)

ThreonineThreonine (Thr or T)(Thr or T)


CC CC

OO

OO––

CHCH33SSCHCH22CHCH22

HH

HH33NN++

MethionineMethionine(Met or M)(Met or M)

Methionine Methionine (Met or M)(Met or M)


CC CC

OO

OO––

CHCH22SSHH

HH

HH33NN++

CysteineCysteine(Cys or C)(Cys or C)

Cysteine Cysteine (Cys or C)(Cys or C)


Aspartic AcidAspartic Acid

CC CC

OO

OO––HH

HH33NN++

OCCHOCCH22

OO

––

(Asp or D)(Asp or D)

Aspartic Acid Aspartic Acid (Asp or D)(Asp or D)


AsparagineAsparagine

CC CC

OO

OO––HH

HH33NN++

HH22NCCHNCCH22

OO

(Asn or N)(Asn or N)

Asparagine Asparagine (Asn or N)(Asn or N)


Glutamic AcidGlutamic Acid

CC CC

OO

OO––HH

HH33NN++

OCCHOCCH22CHCH22

OO

––

(Glu or E)(Glu or E)

Glutamic Acid Glutamic Acid (Glu or E)(Glu or E)


GlutamineGlutamine

CC CC

OO

OO––HH

HH33NN++

HH22NCCHNCCH22CHCH22

OO

(Gln or Q)(Gln or Q)

Glutamine Glutamine (Gln or Q)(Gln or Q)


CC CC

OO

OO––

CHCH22CHCH22CHCH22NNHCHCNNHH22

HH

HH33NN++

ArginineArginine

++ NNHH22

(Arg or R)(Arg or R)

Arginine Arginine (Arg or R)(Arg or R)


CC CC

OO

OO––

CHCH22CHCH22CHCH22CHCH22NNHH33

HH

HH33NN++

LysineLysine

++

(Lys or K)(Lys or K)

Lysine Lysine (Lys or K)(Lys or K)


ProlineProline

CC CC

OO

OO––

CHCH22

HH

HH22NN++

HH22CCCCHH22

(Pro or P)(Pro or P)

Proline Proline (Pro or P)(Pro or P)


PhenylalaninePhenylalanine

CC CC

OO

OO––

CHCH22

HH

HH33NN++

(Phe or F)(Phe or F)

Phenylalanine Phenylalanine (Phe or F)(Phe or F)


TyrosineTyrosine

CC CC

OO

OO––

CHCH22

HH

HH33NN++

OHOH

(Tyr or Y)(Tyr or Y)

Tyrosine Tyrosine (Tyr or Y)(Tyr or Y)


TryptophanTryptophan

CC CC

OO

OO––

CHCH22

HH

HH33NN++

NN

HH

(Trp or W)(Trp or W)

Tryptophan Tryptophan (Trp or W)(Trp or W)


HistidineHistidine

CC CC

OO

OO––HH

HH33NN++

CHCH22 NHNHNN

(His or H)(His or H)

Histidine Histidine (His or H)(His or H)

Amino Acids:Amino Acids:

SelenocysteineSelenocysteine

CH2

CH

CHO O

Se

H

SelenocysteineSelenocysteine


Pyrrolysine (4 R, 5 R)Pyrrolysine (4 R, 5 R)

N

N

H

2

C

O

2

H

N

H

C

O

X

C

H

3

N

H

2

O

H

X

=

PyrrolysinePyrrolysine

Acid-Base Behavior of Amino AcidsAcid-Base Behavior of Amino Acids


While their name implies that amino acids are While their name implies that amino acids are compounds that contain an —NHcompounds that contain an —NH2 2 group and a group and a —CO—CO22H group, these groups are actually H group, these groups are actually present as —NHpresent as —NH33

++ and —CO and —CO22–– respectively. respectively.

How do we know this?How do we know this?

Properties of GlycineProperties of Glycine

OO

OHOHHH22NNCHCH22CC••••

••••••••

•••• ••••––••••

OO

OOHH33NNCHCH22CC ••••••••

•••• ••••++

The properties of glycine:The properties of glycine:

high melting point (when heated to 233°C it high melting point (when heated to 233°C it decomposes before it melts)decomposes before it melts)solubility: soluble in water; not soluble in solubility: soluble in water; not soluble in nonpolar solventnonpolar solvent

more consistent with thismore consistent with this than thisthan this

Properties of GlycineProperties of Glycine

––••••

OO


•••• ••••++

The properties of glycine:The properties of glycine:

high melting point (when heated to 233°C it high melting point (when heated to 233°C it decomposes before it melts)decomposes before it melts)solubility: soluble in water; not soluble in solubility: soluble in water; not soluble in nonpolar solventnonpolar solvent

more consistent with thismore consistent with thiscalled a called a zwitterionzwitterion or or

dipolar iondipolar ion

Acid-Base Properties of GlycineAcid-Base Properties of Glycine

The zwitterionic structure of glycine also follows The zwitterionic structure of glycine also follows from considering its acid-base properties.from considering its acid-base properties.

A good way to think about this is to start with the A good way to think about this is to start with the structure of glycine in strongly acidic solution, structure of glycine in strongly acidic solution, say pH = 1.say pH = 1.

At pH = 1, glycine exists in its protonated form At pH = 1, glycine exists in its protonated form (a monocation).(a monocation).


The zwitterionic structure of glycine also follows The zwitterionic structure of glycine also follows from considering its acid-base properties.from considering its acid-base properties.

A good way to think about this is to start with the A good way to think about this is to start with the structure of glycine in strongly acidic solution, structure of glycine in strongly acidic solution, say pH = 1.say pH = 1.

At pH = 1, glycine exists in its protonated form At pH = 1, glycine exists in its protonated form (a monocation).(a monocation).

OO

OHOHHH33NNCHCH22CC++

••••••••

•••• ••••


Now ask yourself "As the pH is raised, which is Now ask yourself "As the pH is raised, which is the first proton to be removed? Is it the proton the first proton to be removed? Is it the proton attached to the positively charged nitrogen, or is attached to the positively charged nitrogen, or is it the proton of the carboxyl group?"it the proton of the carboxyl group?"

You can choose between them by estimating You can choose between them by estimating their respective ptheir respective pKKaas.s.

OO


••••••••

•••• ••••


Now ask yourself "As the pH is raised, which is Now ask yourself "As the pH is raised, which is the first proton to be removed? Is it the proton the first proton to be removed? Is it the proton attached to the positively charged nitrogen, or is attached to the positively charged nitrogen, or is it the proton of the carboxyl group?"it the proton of the carboxyl group?"

You can choose between them by estimating You can choose between them by estimating their respective ptheir respective pKKaas.s.

OO


••••••••

•••• ••••

typical typical ammonium ammonium ion: pion: pKKaa ~9 ~9

typical typical carboxylic carboxylic acid: pacid: pKKaa ~5 ~5


The more acidic proton belongs to the COThe more acidic proton belongs to the CO22H H group. It is the first one removed as the pH is group. It is the first one removed as the pH is raised.raised.

OO


••••••••

•••• ••••



Therefore, the more stable neutral form of Therefore, the more stable neutral form of glycine is the zwitterion.glycine is the zwitterion.

OO


••••••••

•••• ••••


––••••

OO


•••• ••••++

The measured pThe measured pKKaa of glycine is 2.34. of glycine is 2.34.

Glycine is stronger than a typical carboxylic acid Glycine is stronger than a typical carboxylic acid because the positively charged N acts as an because the positively charged N acts as an electron-withdrawing, acid-strengthening electron-withdrawing, acid-strengthening substituent on the substituent on the carbon. carbon.


OO


••••••••

•••• ••••



––••••

OO


•••• ••••++

The pThe pKKaa for removal of this proton is 9.60. for removal of this proton is 9.60.This value is about the same as that for NHThis value is about the same as that for NH44

++

HOHO––––••••

OO


•••• ••••••••

A proton attached to N in the zwitterionic form of A proton attached to N in the zwitterionic form of nitrogen can be removed as the pH is increased nitrogen can be removed as the pH is increased further. further.

Isoelectric Point pIsoelectric Point pII

––••••

OO


•••• ••••++

––••••

OO


•••• ••••••••

OO


••••••••

•••• ••••

ppKKaa = 2.34 = 2.34

ppKKaa = 9.60 = 9.60

The pH at which the The pH at which the concentration of the concentration of the zwitterion is a zwitterion is a maximum is called the maximum is called the isoelectric pointisoelectric point. Its . Its numerical value is the numerical value is the average of the two average of the two ppKKaas.s.

The pI of glycine is The pI of glycine is 5.97.5.97.

Acid-Base Properties of Amino AcidsAcid-Base Properties of Amino Acids

One way in which amino acids differ is in One way in which amino acids differ is in respect to their acid-base properties. This is the respect to their acid-base properties. This is the basis for certain experimental methods for basis for certain experimental methods for separating and identifying them.separating and identifying them.

Just as important, the difference in acid-base Just as important, the difference in acid-base properties among various side chains affects properties among various side chains affects the properties of the proteins that contain them.the properties of the proteins that contain them.

Amino Acids with Neutral Side ChainsAmino Acids with Neutral Side Chains

CC CC

OO

OO––

HH

HH

HH33NN++

GlycineGlycineppKKa1a1 = = 2.342.34ppKKa2a2 == 9.609.60pIpI == 5.975.97


AlanineAlanineppKKa1a1 = = 2.342.34ppKKa2a2 == 9.699.69ppI I == 6.006.00

HH33NN CC CC

OO

OO––

CHCH33

HH++


ValineValineppKKa1a1 = = 2.322.32ppKKa2a2 == 9.629.62ppI I == 5.965.96

HH33NN CC CC

OO

OO––

CH(CHCH(CH33))22

HH++


LeucineLeucineppKKa1a1 = = 2.362.36ppKKa2a2 == 9.609.60ppI I == 5.985.98

HH33NN CC CC

OO

OO––

CHCH22CH(CHCH(CH33))22

HH++


IsoleucineIsoleucineppKKa1a1 = = 2.362.36ppKKa2a2 == 9.609.60ppI I == 5.985.98

HH33NN CC CC

OO

OO––

CHCH33CHCHCHCH22CHCH33

HH++


MethionineMethionineppKKa1a1 = = 2.282.28ppKKa2a2 == 9.219.21ppI I == 5.745.74

HH33NN CC CC

OO

OO––

CHCH33SSCHCH22CHCH22

HH++


ProlineProlineppKKa1a1 = = 1.991.99ppKKa2a2 == 10.6010.60ppI I == 6.306.30

HH22NN CC CC

OO

OO––HH

++

CHCH22HH22CCCCHH22

Side ChainsSide Chains

PhenylalaninePhenylalanineppKKa1a1 = = 1.831.83ppKKa2a2 == 9.139.13ppI I == 5.485.48

HH33NN CC CC

OO

OO––HH

++

CHCH22


TryptophanTryptophanppKKa1a1 = = 2.832.83ppKKa2a2 == 9.399.39ppI I == 5.895.89

HH33NN CC CC

OO

OO––HH

++

CHCH22 HH

NN


AsparagineAsparagineppKKa1a1 = = 2.022.02ppKKa2a2 == 8.808.80ppI I == 5.415.41

HH33NN CC CC

OO

OO––HH

++

HH22NCCHNCCH22

OO


GlutamineGlutamineppKKa1a1 = = 2.172.17ppKKa2a2 == 9.139.13ppI I == 5.655.65

HH33NN CC CC

OO

OO––HH

++

HH22NCCHNCCH22CHCH22

OO


SerineSerineppKKa1a1 = = 2.212.21ppKKa2a2 == 9.159.15ppI I == 5.685.68

HH33NN CC CC

OO

OO––

CHCH22OHOH

HH++


ThreonineThreonineppKKa1a1 = = 2.092.09ppKKa2a2 == 9.109.10ppI I == 5.605.60

HH33NN CC CC

OO

OO––

CHCH33CHOHCHOH

HH++

Amino Acids with Ionizable Side ChainsAmino Acids with Ionizable Side Chains

Aspartic acidAspartic acidppKKa1a1 = = 1.881.88ppKKa2a2 == 3.653.65ppKKa3a3 == 9.60 9.60 ppI I == 2.772.77

HH33NN CC CC

OO

OO––HH

++

OCCHOCCH22

OO

––

For amino acids with acidic side chains, pI is the For amino acids with acidic side chains, pI is the average of paverage of pKKa1a1 and p and pKKa2a2..


Glutamic acidGlutamic acidppKKa1a1 = = 2.192.19ppKKa2a2 == 4.254.25ppKKa3a3 == 9.67 9.67 ppI I == 3.223.22

HH33NN CC CC

OO

OO––HH

++

OO

OCCHOCCH22CHCH22––


TyrosineTyrosineppKKa1a1 = = 2.202.20ppKKa2a2 == 9.119.11ppKKa3a3 == 10.07 10.07 ppI I == 5.665.66

HH33NN CC CC

OO

OO––HH

++

CHCH22 OHOH


CysteineCysteine HH33NN CC CC

OO

OO––

CHCH22SSHH

HH++ ppKKa1a1 = = 1.961.96

ppKKa2a2 == 8.188.18ppKKa3a3 == 10.28 10.28 ppI I == 5.075.07


LysineLysine

ppKKa1a1 = = 2.182.18ppKKa2a2 == 8.958.95ppKKa3a3 == 10.5310.53ppI I == 9.749.74

HH33NN CC CC

OO

OO––HH

++

CHCH22CHCH22CHCH22CHCH22NNHH33

++

For amino acids with basic side chains, pI is the For amino acids with basic side chains, pI is the average of paverage of pKKa2a2 and p and pKKa3a3..


ArginineArginine

ppKKa1a1 = = 2.172.17ppKKa2a2 == 9.049.04ppKKa3a3 == 12.4812.48ppI I == 10.7610.76

HH33NN CC CC

OO

OO––HH

++

CHCH22CHCH22CHCH22NNHCHCNNHH22

++ NNHH22


HistidineHistidineppKKa1a1 = = 1.821.82ppKKa2a2 == 6.006.00ppKKa3a3 == 9.17 9.17 ppI I == 7.597.59

HH33NN CC CC

OO

OO––HH

++

CHCH22 NHNHNN

Stereochemistry of Amino AcidsStereochemistry of Amino Acids

Configuration of Configuration of -Amino Acids-Amino Acids

Glycine is achiral. All of the other amino acids Glycine is achiral. All of the other amino acids in proteins have the in proteins have the LL-configuration at their -configuration at their carbon.carbon.

HH33NN++

HH

RR

COCO22––

ProteinsProteinsAmino AcidsAmino AcidsOur bodies can synthesize about 10 amino acids.Our bodies can synthesize about 10 amino acids.

Essential amino acids are the other 10 amino acids, which Essential amino acids are the other 10 amino acids, which have to be ingested.have to be ingested.

The The -carbon in all amino acids except glycine is chiral (has -carbon in all amino acids except glycine is chiral (has 4 different groups attached to it).4 different groups attached to it).

Chiral molecules exist as two non-superimposable mirror Chiral molecules exist as two non-superimposable mirror images.images.

The two mirror images are called enantiomers.The two mirror images are called enantiomers.

Chiral molecules can rotate the plane of polarized light.Chiral molecules can rotate the plane of polarized light.

ProteinsProteinsAmino AcidsAmino Acids

ProteinsProteins

Amino AcidsAmino AcidsThe enantiomer that rotates the plane of polarized light to The enantiomer that rotates the plane of polarized light to the left is called L- (the left is called L- (laevus laevus = “left”) and the other = “left”) and the other enantiomer is called D- (enantiomer is called D- (dexterdexter = right). = right).

Enantiomers have identical physical and chemical Enantiomers have identical physical and chemical properties. They only differ in their interaction with other properties. They only differ in their interaction with other enantiomers. enantiomers.

Most amino acids in proteins exist in the L-form.Most amino acids in proteins exist in the L-form.

ProteinsProteinsPolypeptides and ProteinsPolypeptides and ProteinsProteins are polyamides.Proteins are polyamides.

When formed by amino acids, each amide group is called When formed by amino acids, each amide group is called a peptide bond.a peptide bond.

Peptides are formed by condensation of the -COOH group Peptides are formed by condensation of the -COOH group of one amino acid and the NH group of another amino of one amino acid and the NH group of another amino acid.acid.

The acid forming the peptide bond is named first. The acid forming the peptide bond is named first. Example: if a dipeptide is formed from alanine and glycine Example: if a dipeptide is formed from alanine and glycine so that the COOH group of glycine reacts with the NH so that the COOH group of glycine reacts with the NH group of alanine, then the dipeptide is called glycylalanine.group of alanine, then the dipeptide is called glycylalanine.

ProteinsProteinsPolypeptides and ProteinsPolypeptides and ProteinsGlycylalanine is abbreviated gly-ala or GA.Glycylalanine is abbreviated gly-ala or GA.

Polypeptides are formed with a large number of amino Polypeptides are formed with a large number of amino acids (usually result in proteins with molecular weights acids (usually result in proteins with molecular weights between 6000 and 50 million amu).between 6000 and 50 million amu).

Protein StructureProtein StructurePrimary structure is the sequence of the amino acids Primary structure is the sequence of the amino acids in the protein.in the protein.

A change in one amino acid can alter the biochemical A change in one amino acid can alter the biochemical behavior of the protein.behavior of the protein.

Protein StructureProtein Structure

11oo : The linear sequence of amino acids and disulfide : The linear sequence of amino acids and disulfide bonds eg. ARDV:Alabonds eg. ARDV:Ala..ArgArg..AspAsp..Val. Val.

22oo : Local structures which include, folds, turns, : Local structures which include, folds, turns, --helices and helices and -sheets held in place by hydrogen bonds.-sheets held in place by hydrogen bonds.

33oo : : 3-D3-D arrangement of all atoms in a single polypeptide arrangement of all atoms in a single polypeptide chain. chain.

44oo : Arrangement of polypeptide chains into a functional : Arrangement of polypeptide chains into a functional protein, eg. hemoglobin.protein, eg. hemoglobin.

EnzymesEnzymes

Enzymes are proteins which act as biological catalysts.Enzymes are proteins which act as biological catalysts.

Over 1500 have been isolated.Over 1500 have been isolated.

Human genome project scientists estimate that there Human genome project scientists estimate that there are about 30,000 (>100,000) enzymes in a human.are about 30,000 (>100,000) enzymes in a human.

Active (catalytic) site is a crevice which binds a Active (catalytic) site is a crevice which binds a substrate. Lock & key metaphore ....but, protein can substrate. Lock & key metaphore ....but, protein can change conformation.change conformation.

The active site is evolutionarily conserved. The active site is evolutionarily conserved.

Enzyme Inhibitors / EffectorsEnzyme Inhibitors / EffectorsMichaelis-Minton KineticsMichaelis-Minton Kinetics

E = Enzyme; S = SubstrateE = Enzyme; S = Substrate

Enzyme Activity is reduced by inhibitors.Enzyme Activity is reduced by inhibitors.

Four types of inhibitors:Four types of inhibitors:Reversible, Irreversible, Competitive, Non-competitiveReversible, Irreversible, Competitive, Non-competitive

Equilibrium Constant & Free EnergyEquilibrium Constant & Free EnergyKK[ES]eq[ES]eq = 10 = 10-2 -2 to 10to 10-6 -6 ; ; Free Energies -3 to -12 kcal/molFree Energies -3 to -12 kcal/molvs. covalent bonds -50 to -110 kcal/molvs. covalent bonds -50 to -110 kcal/mol

Effectors increase enzyme activity.Effectors increase enzyme activity.

E + S [ES] E + Product

Amino Acids & Proteins

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