Amino Acids (2) IUA

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.
TheCarboxylgroupshavepKa valuesofbetween1.8and y g p p 2.8(moreacidicthansimplemonocarboxylic acids).
TheaminogroupshavepKa valuesbetween8.8and10.6, g p p , dependingontheaminoacid.
Acidicandbasicaminoacidshaveadditionalionizable groups.
AtifHassanKhirelsied
AminoAcidshavedistinctdissociationcurves
Atitsisoelectric pH(pI),anaminoacidbearsnonet charge(Zwitterion) charge (Zwitterion)
Atitsisoelectric pH(pI),anaminoacidbearsnonet charge
Thebufferingactionofaminoacids
Reactionsofaminoacids
Reactionsofaminoacids
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
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.
Peptidesandproteins
Proteinsarepolymers ofaminoacidsjoinedbypeptide bonds.
Peptidesandproteins
The peptide bond exhibits partial double-bond character character.
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.
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
The secondary structure.
The two most common types of secondary structure, the -helix and the -sheet,
-helix
The -helix
Stabilized by hydrogen bonds Compact C t
The sheet The sheet
Stabilized by hydrogen bonds Is highly extended. Either Eith parallel or antiparallel. ll l ti ll l
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.
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.
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.
The quaternary structure
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
The forces that stabilize proteins structure p
Some proteins contain covalent disulfide (S-S) bonds that link the sulfhydryl groups of cysteinyl residues.
Proteinsdenaturation
Denaturation:isthereversibleruptureofthenon covalentbondsinproteinmoleculeswhichresultsinloss covalent bonds in protein molecules which results in loss ofproteinconformationandbiologicalactivity.
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.

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AminoAcids(2)

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

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

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

Atitsisoelectric pH(pI),anaminoacidbearsnonet charge

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

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

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