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Protein Science, Vol 7, Issue 12 2533-2540, Copyright © 1998 by Cold Spring Harbor Laboratory Press
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T. SZYPERSKI, G. VANDENBUSSCHE, T. CURSTEDT, J. M. RUYSSCHAERT, K. WUTHRICH and J. JOHANSSON
Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule Honggerberg, CH-8093 Zurich, Switzerland
In the 35-residue pulmonary surfactant-associated lipopolypeptide C (SP-C), the stability of the valyl-rich {alpha}-helix comprising residues 9-34 has been monitored by circular dichroism, nuclear magnetic resonance, and Fourier transform infrared spectroscopy in both a mixed organic solvent and in phospholipid micelles. The {alpha}-helical form of SP-C observed in freshly prepared solutions in a mixed solvent of CHCl(3)/CH(3)OH/0.1 M HCl 32:64:5 (v/v/v) at 10{deg}C undergoes within a few days an irreversible transformation to an insoluble aggregate that contains {beta}-sheet secondary structure. Hydrogen exchange experiments revealed that this conformational transition proceeds through a transition state with an Eyring free activation enthalpy of about 100 kJ mol(-1), in which the polypeptide segment 9-27 largely retains a helical conformation. In dodecylphosphocholine micelles, the helical form of SP-C was maintained after seven weeks at 50{deg}C. The {alpha}-helical form of SP-C thus seems to be the thermodynamically most stable state in this micellar environment, whereas its presence in freshly prepared samples in the aforementioned mixed solvent is due to a high kinetic barrier for unfolding. These observations support a previously proposed pathway for in vivo synthesis of SP-C through proteolytic processing from a 21-kDa precursor protein.
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