Pages that link to "Q35604909"
The following pages link to Controlling the pKa of the bacteriorhodopsin Schiff base by use of artificial retinal analogues (Q35604909):
Displaying 43 items.
- Deformation of helix C in the low temperature L-intermediate of bacteriorhodopsin (Q27642312) (← links)
- Elucidating the exact role of engineered CRABPII residues for the formation of a retinal protonated Schiff base (Q27656422) (← links)
- Deprotonation of D96 in Bacteriorhodopsin Opens the Proton Uptake Pathway (Q27676244) (← links)
- Rational Design of a Colorimetric pH Sensor from a Soluble Retinoic Acid Chaperone (Q27680022) (← links)
- A Photoisomerizing Rhodopsin Mimic Observed at Atomic Resolution (Q27711181) (← links)
- Retinal conformation governs pKa of protonated Schiff base in rhodopsin activation (Q28818812) (← links)
- Light-Activated Reversible Imine Isomerization: Towards a Photochromic Protein Switch (Q28834593) (← links)
- pH-Dependent absorption spectrum of a protein: a minimal electrostatic model of Anabaena sensory rhodopsin (Q30402109) (← links)
- A large photolysis-induced pKa increase of the chromophore counterion in bacteriorhodopsin: implications for ion transport mechanisms of retinal proteins (Q30447600) (← links)
- The protonation-deprotonation kinetics of the protonated Schiff base in bicelle bacteriorhodopsin crystals (Q31158820) (← links)
- Energetics and dynamics of a light-driven sodium-pumping rhodopsin (Q33887063) (← links)
- Studies of cation binding in ZnCl2-regenerated bacteriorhodopsin by x-ray absorption fine structures: effects of removing water molecules and adding Cl- ions (Q33907633) (← links)
- Effect of intermolecular orientation upon proton transfer within a polarizable medium (Q34088015) (← links)
- Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: a resonance Raman study of the Schiff base hydrogen/deuterium exchange (Q34115159) (← links)
- Octopus photoreceptor membranes. Surface charge density and pK of the Schiff base of the pigments (Q34126339) (← links)
- Voltage Dependence of Proton Pumping by Bacteriorhodopsin Is Regulated by the Voltage-Sensitive Ratio of M1 to M2 (Q34167136) (← links)
- Molecular dynamics study of the nature and origin of retinal's twisted structure in bacteriorhodopsin. (Q34172353) (← links)
- The voltage-dependent proton pumping in bacteriorhodopsin is characterized by optoelectric behavior (Q34176538) (← links)
- Schiff base switch II precedes the retinal thermal isomerization in the photocycle of bacteriorhodopsin (Q34904556) (← links)
- Bacteriorhodopsin: a high-resolution structural view of vectorial proton transport (Q34985051) (← links)
- Structural and mechanistic insight from high resolution structures of archaeal rhodopsins (Q35589971) (← links)
- A three-dimensional movie of structural changes in bacteriorhodopsin (Q36232010) (← links)
- The all-trans-retinal dimer series of lipofuscin pigments in retinal pigment epithelial cells in a recessive Stargardt disease model. (Q36288534) (← links)
- Uptake and protein targeting of fluorescent oxidized phospholipids in cultured RAW 264.7 macrophages. (Q37216241) (← links)
- Electric-field-induced Schiff-base deprotonation in D85N mutant bacteriorhodopsin (Q37261831) (← links)
- On the molecular mechanisms of the Schiff base deprotonation during the bacteriorhodopsin photocycle (Q37407382) (← links)
- Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation (Q37684251) (← links)
- Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base (Q37684380) (← links)
- Protein modification by aldehydophospholipids and its functional consequences (Q37997263) (← links)
- Synthetic retinals as probes for the binding site and photoreactions in rhodopsins (Q38758862) (← links)
- Studies of rhodopsin and bacteriorhodopsin using modified retinals (Q39762500) (← links)
- A role for internal water molecules in proton affinity changes in the Schiff base and Asp85 for one-way proton transfer in bacteriorhodopsin (Q40058430) (← links)
- The unusual pK(a) of the rhodopsin chromophore: Is this how nature minimizes photoreceptor noise? (Q41776973) (← links)
- pKa of the protonated Schiff base of bovine rhodopsin. A study with artificial pigments (Q41975196) (← links)
- The pKa of the protonated Schiff bases of gecko cone and octopus visual pigments (Q42184646) (← links)
- Evidence for a controlling role of water in producing the native bacteriorhodopsin structure (Q42929056) (← links)
- Combining ab initio quantum mechanics with a dipole-field model to describe acid dissociation reactions in water: first-principles free energy and entropy calculations (Q43156502) (← links)
- Synthesis of N-heteroaryl retinals and their artificial bacteriorhodopsins. (Q46758259) (← links)
- Modulation of spectral properties and pump activity of proteorhodopsins by retinal analogues (Q50452276) (← links)
- Synthetic retinal analogues modify the spectral and kinetic characteristics of microbial rhodopsin optogenetic tools. (Q51025337) (← links)
- Performance of the AM1, PM3, and SCC-DFTB methods in the study of conjugated Schiff base molecules (Q57233451) (← links)
- The dielectric effect of the environment on the p K a of the retinal Schiff base and on the stabilization of the ion pair in bacteriorhodopsin (Q57233470) (← links)
- Electronic State Mixing Controls the Photoreactivity of a Rhodopsin with all- trans Chromophore Analogues (Q57798227) (← links)