basicity of some amines aminekbpkb ammonia nh 3 1.80e-054.74 propylamine ch 3 ch 2 ch 2 nh 2...
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![Page 1: 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](https://reader035.vdocuments.us/reader035/viewer/2022062404/551a8d53550346e0158b4f8a/html5/thumbnails/1.jpg)
Basicity of some amines
Amine Kb pKbAmmonia NH3 1.80E-05 4.74
Propylamine CH3CH2CH2NH2 4.70E-04 3.33
2-Propylamine (CH3) 2CHNH2 3.40E-04 3.47
Methylamine CH3NH2 4.40E-04 3.36
Dimethylamine (CH3) 2NH 5.40E-04 3.27
Trimethylamine (CH3) 3N 5.90E-05 4.23
Aniline C6H5NH2 3.80E-10 9.42
4-Methylaniline 4-CH3C6H4NH2 1.20E-09 8.92
2-Nitroaniline 1.50E-15 14.82
3-Nitroaniline 2.80E-13 12.55
4-Nitroaniline 9.50E-14 13.02
2
B + H2O HB+ + OH- Kb = a(HB+) x a((OH-)/[a(B) x a(H2O)]
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The 21 amino acids found in eukaryotes.
(Grouped according to their side-chains' pKa values and charge at physiological pH 7.4)
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The peptide bond
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Polymerisation of ε-caprolactam to a polyamide (Nylon-6)
O
H2O
-Aminocapronsäure
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CH
CHN
O
N
CH2
SH
O
CH
CH2
CHN
O
N
OCH2
OH
H
H H
H
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a-helix
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Primary structure: Amino acid sequence in a polypeptide (protein)
amino acids
CH
CHNH
O
NH
CH2
SH
O
OHCH
CH2
CHNH
O
NH
OCH2
OH
![Page 8: 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](https://reader035.vdocuments.us/reader035/viewer/2022062404/551a8d53550346e0158b4f8a/html5/thumbnails/8.jpg)
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.
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3D structure of the protein myoglobin showing colored alpha helices.
hemeprosthetic group, co-factor
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Beta-meander motifPortion of outer surface Protein A of Borrelia burgdorferi complexed with a murine monoclonal antibody.
Psi-loop motifPortion of Carboxypeptidase A.
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Die vier Ebenen der Proteinstruktur, von links nach rechts: Primärstruktur, Sekundärstruktur (β-Faltblatt unten, α-Helix oben), Tertiär- und Quartärstruktur.
a-helix-sheet
primary secondary tertiary quaternary
structure
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The crystal structure of the chaperonin. Chaperonins assist protein folding.
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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)