Auerbach G, Gaill F, Jaenicke R, Schulthess T, Timpl R, Engel J
Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.
Matrix Biol. 1995 Jul;14(7):589-92. doi: 10.1016/s0945-053x(05)80008-3.
Calf skin collagen type I and interstitial collagen of the annelids Alvinella pompejana and Riftia pachyptila were thermally unfolded at pressures of 1 and 200 bar. The high pressure was near the habitat pressure of the annelids which live in deep sea hydrothermal vents. The transition temperature increased with pressure by only 1.4 +/- 1 degrees C for calf skin collagen, and no pressure effect was detectable for the annelid collagens. The value for calf skin collagen agrees with prediction based on published values of the transition volume and transition enthalpy. The triple helices of the interstitial collagens of the annelids, which have melting temperatures of 46 degrees C (Alivinella pompejana) and 29 degrees C (Riftia pachyptila), are not further stabilized by pressure.