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Basicity of some amines AmineKbpKb Ammonia NH 3 1.80E-054.74 Propylamine CH 3 CH 2 CH 2 NH 2 4.70E-043.33 2-Propylamine (CH 3 ) 2 CHNH 2 3.40E-043.47 Methylamine.

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Presentation on theme: "Basicity of some amines AmineKbpKb Ammonia NH 3 1.80E-054.74 Propylamine CH 3 CH 2 CH 2 NH 2 4.70E-043.33 2-Propylamine (CH 3 ) 2 CHNH 2 3.40E-043.47 Methylamine."— Presentation transcript:

1 Basicity of some amines AmineKbpKb Ammonia NH E Propylamine CH 3 CH 2 CH 2 NH E Propylamine (CH 3 ) 2 CHNH E Methylamine CH 3 NH E Dimethylamine (CH 3 ) 2 NH5.40E Trimethylamine (CH 3 ) 3 N5.90E Aniline C 6 H 5 NH E Methylaniline 4-CH 3 C 6 H 4 NH E Nitroaniline1.50E Nitroaniline2.80E Nitroaniline9.50E B + H 2 O HB + + OH - K b = a(HB + ) x a((OH - )/[a(B) x a(H 2 O)]

2 The 21 amino acids found in eukaryotes. (Grouped according to their side-chains' pKa values and charge at physiological pH 7.4)

3 The peptide bond

4 Polymerisation of ε-caprolactam to a polyamide (Nylon-6) O H2OH2O  -Aminocapronsäure

5

6 a -helix

7 Primary structure: Amino acid sequence in a polypeptide (protein) amino acids

8 Hemoglobin (English pronunciation: /hiːməˈgloʊbɪn/; also spelled haemoglobin and abbreviated Hb or Hgb) is the iron-containing oxygen- transport metalloprotein in the red blood cells of all vertebrates.

9 3D structure of the protein myoglobin showing colored alpha helices. heme prosthetic group, co-factor

10 Beta-meander motif Portion of outer surface Protein A of Borrelia burgdorferi complexed with a murine monoclonal antibody. Psi-loop motif Portion of Carboxypeptidase A.

11 Die vier Ebenen der Proteinstruktur, von links nach rechts: Primärstruktur, Sekundärstruktur (β-Faltblatt unten, α-Helix oben), Tertiär- und Quartärstruktur. a -helix  -sheet primarysecondarytertiaryquaternary structure

12 The crystal structure of the chaperonin. Chaperonins assist protein folding.

13 Three possible representations of the three-dimensional structure of the protein triose phosphate isomerase. Left: all-atom representation colored by atom type. Middle: Simplified representation illustrating the backbone conformation, colored by secondary structure. Right: Solvent-accessible surface representation colored by residue type (acidic residues red, basic residues blue, polar residues green, nonpolar residues white)


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