<bos><start_of_turn>system
You are a helpful AI assistant.
lista de codigos linguisticos disponibles: ["en", "es"].<end_of_turn>
<start_of_turn>user
I want to submit an article to the Journal of Structural Biology. The abstract is as follows:

Transthyretin (TTR) is a tetrameric protein associated with human amyloidosis. In vitro, the formation of amyloid fibrils by TTR is known to be promoted by low pH. Here we show the neutron structure of TTR, focusing on the hydrogen bonds, protonation states, and pH sensitivities. A large crystal was prepared at pD 7.4 for neutron protein crystallography. Neutron diffraction studies were conducted using the IBARAKI Biological Crystal Diffractometer with the time-of-flight method. The neutron structure solved at 2.0Å resolution revealed the protonation states of His88 and the detailed hydrogen-bond network depending on the protonation states of His88. This hydrogen-bond network is composed of Thr75, Trp79, His88, Ser112, Pro113, Thr118-B, and four water molecules and is involved in both monomer-monomer and dimer-dimer interactions, suggesting that the double protonation of His88 by acidification breaks the hydrogen-bond network and causes the destabilization of the TTR tetramer. In addition, the comparison with X-ray structure at pH 4.0 indicated that protonation occurred to Asp74, His88, and Glu89 at pH 4.0. Our neutron model provides insights into the molecular stability of TTR related to the hydrogen-bond network, the pH sensitivity, and the CH2O weak hydrogen bond.

Please give me a good title suggestion.<end_of_turn>
<start_of_turn>model
Por supuesto, una de las posibles opciones de título es "Red de enlaces de hidrógeno y sensibilidad al pH en la transtiretina: estructura cristalina de neutrones de la transtiretina humana".<end_of_turn><eos>