Introduction to Protein JL LO & HC Lee 2000 June-July.
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Transcript of Introduction to Protein JL LO & HC Lee 2000 June-July.
![Page 1: Introduction to Protein JL LO & HC Lee 2000 June-July.](https://reader030.fdocuments.net/reader030/viewer/2022032800/56649d395503460f94a12df9/html5/thumbnails/1.jpg)
Introduction to Protein
JL LO & HC Lee2000 June-July
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Gene & Protein
• One gene, one protein• ..\talks\protein_3.ps
• Genotype & phenotype• ..\talks\protein_4.ps
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What do proteins do?
• Everything
• Structural and Functional
• Structural– blood, muscle, bone, etc.
• Functional – metabolic, neural, reproduction
Aberrant gene > malfunction protein > disease
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• 20 amino acids are coded by groups of three bases (triplets or CODONS)
• Bases are: C, T, U (instead of A), G
– 4x4x4 = 64• 3 are stop codons
• 61 code amino acids (with degeneracy)
The Genetic Code I
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The Genetic Code II
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The Genetic Code III
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The Amino Acids
• Single and 3-letter Codes
• Aspartic Acid Asp D Glutamic Acid Glu E • Phenylanine Phe F Glycine Gly G • Alanine Ala A Cysteine Cys C • Histidine His H Isoleucine Ile I • Lysine Lys K Leucine Leu L • Methionine Met M Asparagine Asn N • Proline Pro P Glutamine Gln Q • Arginine Arg R Serine Ser S • Threonine Thr T Valine Val V• Tryptophan Trp W Tyrosine Tyr
Y
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Alanine
Grey - carbon
White - hydrogen
Blue – nitrogen
Red – oxygen
Carboxylic acid group
Amine groupAlpha carbon
Side chain
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The CORN Law
alpha Carbon
cabOxylic acid group
side chain (R)
amiNe group
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Two AminoAcids = 2 x (CORN) – > Dipeptide + Water
(NCR) –CO2- + NH3
+ –(CRO)
= (N – C – R) – C=O
| peptide bond
H – N – (C – R – O) + H2O
Peptide Synthesis
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Polypeptide – chain of peptides
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Hydrophobic-Aliphatic
• Ala(A)
• Val(V)
• Leu(L)
• Ile (I)
• Mostly are bifurcated except Ala
Classification of Amino Acid Side Chains
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Hydrophobic-aromatic
• Phe(F)
• Tyr(Y)
• Trp(W)
• Non-polar
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Neutral-polar side chains
• Ser(S)
• Thr(T)
• Cys(C)
• Met(M)
• Asn(N)
• Gln(Q)
• Possess hydroxyl group
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Acidic amino acids
• Asp(D)
• Glu(E)
• Strongly polar nature
• Catalytic
• Metal ion binding ability
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Basic amino acids
• His(H)
• Lys(K)
• Arg(R)
• Frequently occurring in enzyme
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Conformationally important
• Gly(G)
• Pro(P)
• G has no side chain
• P is the most rigid one
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Peptide Geometry
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Peptide Torsion Angles• Three main chain torsion angle• ψ N - Calpha bond• Ψ C – Calpha bond• ω C – N bond
3D structure of peptide determined if all angles given
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Protein Conformation
..\talks\protein_6.ps ..\talks\protein_7.ps
Alpha-helices
..\..\proteins\1AEP_apolipophorin_III_1.gif
Beta-sheets & coils ..\..\proteins\1FSC_fasciculin_1.gif
1IBA.pdb
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Structure of Alpha-Helix
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Properties of the Alpha-Helix
• A pitch of 5.4 A
• Have 3.6 amino acids residues per turn
• 3.6/5.4=1.5 --- a rise per residue
• Have negative Ψandψangles
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Distortion of Alpha-Helix
• Buries against the other 2nd structure
• Solvent
• 310-helix
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Structure of Beta Sheet• Negative ψand Positive Ψ• Axial distance—3.5 A • Pitch – 7A
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Parallel & Anti-parallel Sheets
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More Examples• ..\..\proteins\1AVH_annexin_V_1.gif
• ..\..\proteins\1ERB_pl_retinol_bp_1.gif
• ..\..\proteins\1ADN_DNA_Repair_1.gif
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Tertiary Structure
• ..\talks\protein_8.ps
• More cartoons of Proteins
• Go to-files
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THE END