Ulrtrafast Water Dynamics in Bacteriorhodopsin
نویسندگان
چکیده
منابع مشابه
Dynamics of water molecules in the bacteriorhodopsin trimer in explicit lipid/water environment.
Protonated networks of internal water molecules appear to be involved in proton transfer in various integral membrane proteins. High-resolution x-ray studies of protein crystals at low temperature deliver mean positions of most internal waters, but only limited information about fluctuations within such H-bonded networks formed by water and residues. The question arises as to how water molecule...
متن کاملRational design of 'water-soluble' bacteriorhodopsin variants.
We have explored the interchangeability of soluble and membrane proteins by attempting to render a helical membrane protein 'water soluble' through mutation of its lipid-exposed residues. Using an atomic resolution structure of bacteriorhodopsin (bR), two different strategies were developed to identify lipid-exposed residues for mutation. In the first strategy all residues in trimeric bR with s...
متن کاملStructures and spectral signatures of protonated water networks in bacteriorhodopsin.
Networks of internal water molecules are thought to provide proton transfer pathways in many enzymatic and photosynthetic reactions. Extremely broad absorption continua observed in recent IR spectroscopic measurements on the photodriven proton pump bacteriorhodopsin (BR) suggest such networks may also serve as proton storage and release sites for these reactions. By combining electronic structu...
متن کاملQuantum dynamics of the femtosecond photoisomerization of retinal in bacteriorhodopsin.
The membrane protein bacteriorhodopsin contains all-trans-retinal in a binding site lined by amino acid side groups and water molecules that guide the photodynamics of retinal. Upon absorption of light, retinal undergoes a subpicosecond all-trans-->13-cis phototransformation involving torsion around a double bond. The main reaction product triggers later events in the protein that induce pumpin...
متن کاملHow environment supports a state: molecular dynamics simulations of two states in bacteriorhodopsin suggest lipid and water compensation.
The light-driven proton pump bacteriorhodopsin (bR) is a transmembrane protein that uses large conformational changes for proton transfer from the cytoplasmic to the extracellular regions. Crystal structures, due to their solvent conditions, do not resolve the effect of lipid molecules on these protein conformational changes. To begin to understand the molecular details behind such large confor...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2014
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2013.11.3393