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Kirchner, H. O. K.

Publications and source records attributed to Kirchner, H. O. K..

2 recordsLinked to original sources

Feather keratin in Pavo cristatus: A tentative structure

The filament of the F-keratin polymer is an alternating arrangement of two tetrameric sequence segments, the "N-block" made of four strands AA 1-52, a twisted parallelepiped and the "C-block", a sandwich of four strands AA 81-100. The N-blocks have 89{degrees}internal rotation within eight levels of {beta}-sandwiches strengthened by three disulfide bonds per monomer. The C-blocks contain 5 aromatic residues, they provide resilience, like vertebral discs in a spinal column. The pitch of an N+C-block octamer is 10 nm. Solidification of F-keratin may involve the "C-blocks" to temporarily mold into "C-wedges" of 18{degrees} tilt, which align the polymer filaments into laterally amorphous fiber-reinforced composites of 9.5 nm axial periodicity. This distance corresponds to the length of the fully stretched AA 53-80 matrix segment. The "spinal column" is deformed like in scoliosis and unwinds under compression when F-keratin filaments perfectly align horizontally and form stacked sheets in the solid state.

biophysics↗

Thermal Decomposition Of The Amino Acids Glycine, Cysteine, Aspartic Acid, Asparagine, Glutamic Acid, Glutamine, Arginine And Histidine

Calorimetry, thermogravimetry and mass spectrometry were used to follow the thermal decomposition of the eight amino acids G, C, D, N, E, Q, R and H between 185{degrees}C and 280{degrees}C. Endothermic heats of decomposition between 72 and 151 kJ/mol are needed to form 12 to 70 % volatile products. This process is neither melting nor sublimation. With exception of cysteine they emit mainly H2O, some NH3 and no CO2. Cysteine produces CO2 and little else. The reactions are described by polynomials, AA ^ a (NH3) + b (H2O) + c (CO2) + d (H2S) + e (residue), with integer or half integer coefficients. The solid monomolecular residues are rich in peptide bonds.

biochemistry↗