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pubmed-article:19187030pubmed:abstractTextWe detect internal water molecules in a membrane-embedded receptor-transducer complex and demonstrate water structure changes during formation of the signaling state. Time-resolved FTIR spectroscopy reveals stimulus-induced repositioning of one or more structurally active water molecules to a significantly more hydrophobic environment in the signaling state of the sensory rhodopsin II (SRII)-transducer (HtrII) complex. These waters, distinct from bound water molecules within the SRII receptor, appear to be in the middle of the transmembrane interface region near the Tyr199(SRII)-Asn74(HtrII) hydrogen bond. We conclude that water potentially plays an important role in the SRII --> HtrII signal transfer mechanism in the membrane's hydrophobic core.lld:pubmed
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pubmed-article:19187030pubmed:articleTitleActive water in protein-protein communication within the membrane: the case of SRII-HtrII signal relay.lld:pubmed
pubmed-article:19187030pubmed:affiliationDepartment of Physics, Molecular Biophysics Laboratory, and Center for Photonics, Boston University, Boston, Massachusetts 02215, USA.lld:pubmed
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