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)]
The 21 amino acids found in eukaryotes. (Grouped according to their side-chains' pKa values and charge at physiological pH 7.4)
The peptide bond
Polymerisation of ε-caprolactam to a polyamide (Nylon-6) O H2OH2O -Aminocapronsäure
a -helix
Primary structure: Amino acid sequence in a polypeptide (protein) amino acids
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.
3D structure of the protein myoglobin showing colored alpha helices. heme prosthetic group, co-factor
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.
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
The crystal structure of the chaperonin. Chaperonins assist protein folding.
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)