AminoAcids(2)

AtifH.Khirelsied,Ph.D. Atif H. Khirelsied, Ph.D.

DepartmentofBiochemistry

FacultyofMedicine
InternationalUniversityofAfrica,Khartoum,Sudan

Acidbasepropertiesofaminoacids

TheaCOOHandaNH2 groupsareionizable. The net electrical charge of an amino acid depends on netelectricalchargeofanaminoaciddependson thepHofthemedium.

Acidbasepropertiesofaminoacids
TheCarboxylgroupshavepKa valuesofbetween1.8and y g p p 2.8(moreacidicthansimplemonocarboxylic acids).

TheaminogroupshavepKa valuesbetween8.8and10.6, g p p , dependingontheaminoacid.

Acidicandbasicaminoacidshaveadditionalionizable groups.
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Acidbasepropertiesofaminoacids

Acidbasepropertiesofaminoacids

AminoAcidshavedistinctdissociationcurves

Atitsisoelectric pH(pI),anaminoacidbearsnonet charge(Zwitterion) charge (Zwitterion)

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Atitsisoelectric pH(pI),anaminoacidbearsnonet charge

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Thebufferingactionofaminoacids

AminoAcidshavedistinctdissociationcurves

AminoAcidshavedistinctdissociationcurves

Reactionsofaminoacids

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Reactionsofaminoacids

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Thepeptidebond p p
A. Anamide CN linkageformingthebackboneofall proteins. B. Involves two adjacent amino acids liked by Involvestwoadjacentaminoacidslikedby eliminationofH2O. C. Planner,i.e.theCNinvolvedlieinthesameplane withtheneighboringatoms with the neighboring atoms

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Thepeptidebond

Theaminoandcarboxyl Th i d b l groupsofaminoacidscan reactinahead to tailfashion react in a headtotail fashion toformpeptides.

Peptidebondformation

Peptidesandproteins p p
Thesimplestpeptide,adipeptide,containsasingle peptidebondformedbythecondensationoftwo peptide bond formed by the condensation of two aminoacidswitheliminationofwater.

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Peptidesandproteins
Proteinsarepolymers ofaminoacidsjoinedbypeptide bonds.

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Peptidesandproteins
The peptide bond exhibits partial double-bond character character.

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Peptidesandproteins

Thenumberandorderofallresiduesinapolypeptide constituteitsprimarystructureoftheprotein. p y p

ProteinStructure

Proteins: ordersofstructure
The Primary structure, the sequence of the amino acids in a polypeptide chain. l tid h i The secondary structure, the folding of short (3- to 30residue), contiguous segments of polypeptide into geometrically ordered units units.

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Proteins: ordersofstructure
The tertiary structure, the three-dimensional assembly of secondary structure units to form larger functional units.

The quaternary structure, the number and types of polypeptide units of oligomeric proteins and th i spatiall arrangement. it f li i t i d their ti t

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Proteins: ordersofstructure
The secondary structure.
The two most common types of secondary structure, the -helix and the -sheet,
-helix

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Proteins: ordersofstructure
The -helix
Stabilized by hydrogen bonds Compact C t

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Proteins: ordersofstructure
The sheet The sheet
Stabilized by hydrogen bonds Is highly extended. Either Eith parallel or antiparallel. ll l ti ll l

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Proteins: ordersofstructure
The tertiary structure
Refers to the three dimensional conformation of a polypeptide polypeptide. Indicates how secondary structural featureshelices, sheets, bends, turns bends turns, and loops are assembled in three-dimensional space three dimensional space, to form domains and how these domains relate spatially to one another.
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Proteins: ordersofstructure
Thequaternarystructure
In some cases, proteins are assembled from more than one polypeptide, protomer. polypeptide or protomer Quaternary structure defines the polypeptide composition of an oligomeric protein protein.

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Proteins: ordersofstructure
The quaternary structure
Dimeric proteins contain two polypeptide chains chains. Homodimers contain two copies of the same p yp p p polypeptide chain, , while in a heterodimer the polypeptides differ. Greek letters (, , etc) are used to distinguish different subunits of a hetero-oligomeric protein.

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Proteins: ordersofstructure
The quaternary structure

Proteins: ordersofstructure
The f Th forces that stabilize proteins structure th t t bili t i t t
Higher orders of protein structure are stabilized primarily by non covalent interactions. non-covalent interactions 1. Hydrophobic interactions. 2. Hydrogen bonds. 3. 3 Salt bridges bridges. 4. van der Waal forces
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Proteins: ordersofstructure
The forces that stabilize proteins structure p
Some proteins contain covalent disulfide (S-S) bonds that link the sulfhydryl groups of cysteinyl residues.

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Proteins: ordersofstructure

Proteinsdenaturation
Denaturation:isthereversibleruptureofthenon covalentbondsinproteinmoleculeswhichresultsinloss covalent bonds in protein molecules which results in loss ofproteinconformationandbiologicalactivity.

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Proteinsdenaturation
Thefunctionofaproteinisabsolutelydependenton itsstructure. its structure. Anumberofagentscandisruptthisstructurethus A number of agents can disrupt this structure thus denaturing theprotein.

Whenaproteinisdenatured,itlosesitsfunction. When a protein is denatured, it loses its function.