Structure of Halorhodopsin from Halobacterium salinarum in a new crystal form that imposes little restraint on the E-F loopStepwise isotope editing of [FeFe]-hydrogenases exposes cofactor dynamicsThe [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron- and carbon dioxide-binding proteins.[NiFe]-hydrogenase maturation: isolation of a HypC-HypD complex carrying diatomic CO and CN- ligands.Structural analysis and mapping of individual protein complexes by infrared nanospectroscopy.Surface Enhanced Resonance Raman Spectroscopy Reveals Potential Induced Redox and Conformational Changes of Cytochrome c Oxidase on Electrodes.Characterisation of subunit III and its oligomer from spinach chloroplast ATP synthase.Proteorhodopsin is a light-driven proton pump with variable vectoriality.Evidence for the isomerization and decarboxylation in the photoconversion of the red fluorescent protein DsRed.Time-resolved Fourier transform infrared study on photoadduct formation and secondary structural changes within the phototropin LOV domainProton transfer reactions across bacteriorhodopsin and along the membrane.In vitro hydrogen production--using energy from the sun.Transient protonation changes in channelrhodopsin-2 and their relevance to channel gatingThe photochemistry of the light-, oxygen-, and voltage-sensitive domains in the algal blue light receptor phot.Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidaseAureochrome 1 illuminated: structural changes of a transcription factor probed by molecular spectroscopyPre-gating conformational changes in the ChETA variant of channelrhodopsin-2 monitored by nanosecond IR spectroscopy.Kinetic and vibrational isotope effects of proton transfer reactions in channelrhodopsin-2Photoactive mitochondria: in vivo transfer of a light-driven proton pump into the inner mitochondrial membrane of Schizosaccharomyces pombe.The molecular mechanism of membrane proteins probed by evanescent infrared waves.High-Field High-Repetition-Rate Sources for the Coherent THz Control of MatterIn-Situ Observation of Membrane Protein Folding during Cell-Free ExpressionNew ultrarapid-scanning interferometer for FT-IR spectroscopy with microsecond time-resolution.Temporal evolution of helix hydration in a light-gated ion channel correlates with ion conductanceBacteriorhodopsin expressed in Schizosaccharomyces pombe pumps protons through the plasma membrane.Protein dynamics observed by tunable mid-IR quantum cascade lasers across the time range from 10ns to 1s.In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopyProtons @ interfaces: implications for biological energy conversion.Biochemical applications of surface-enhanced infrared absorption spectroscopy.Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy.Time-resolved flow-flash FT-IR difference spectroscopy: the kinetics of CO photodissociation from myoglobin revisited.Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins.Thinner, smaller, faster: IR techniques to probe the functionality of biological and biomimetic systems.Surface-enhanced infrared absorption spectroscopy (SEIRAS) to probe monolayers of membrane proteins.Channelrhodopsin unchained: structure and mechanism of a light-gated cation channel.Tailoring the properties and the reactivity of the spinel cobalt oxide.Changes in the hydrogen-bonding strength of internal water molecules and cysteine residues in the conductive state of channelrhodopsin-1.A local area network of protonated water molecules.The protein-tethered lipid bilayer: a novel mimic of the biological membrane.Time-resolved microspectroscopy on a single crystal of bacteriorhodopsin reveals lattice-induced differences in the photocycle kinetics.
P50
Q27700270-CFC6F863-5E35-477A-A7B6-2532F28752F7Q28828282-D8185225-0D9F-4C96-9394-85A9B70253F9Q30317775-29081CBF-E889-4C29-B9B7-CE34500D530CQ30317985-4897BFBC-65B6-476F-A75C-7FD1AC92BA4BQ30356338-72D331F9-128E-4EE9-98B1-C7185A5128E0Q30978215-74A3337E-C4DC-4A1A-A045-7630D37EE5B5Q31029584-45A4A2AF-2B8E-4AA9-89BD-5EB2B21AD441Q31106946-436D8AE9-2BF3-4771-AE92-4919D500F2E0Q33217581-B0BD4B96-7639-4838-BB64-D76C1FE5C446Q33409286-51F949C0-BFBE-4F32-99E9-C6EE404C80A7Q33919262-7B9CB82D-0A7E-430A-987F-C842203D889AQ34151582-045335DB-F137-4CC7-BEA6-A0B2837FAE76Q34333935-CB3C9B85-C0AA-4567-8FE4-B05C9CAA85E1Q34504079-34E8E01F-DCA7-4010-BD66-D0456752A12FQ35170532-B2C809B1-58BE-44A2-A14B-3F712E764B3AQ35212354-5AEA7739-9ABF-4332-9432-8AF9B6FE76CBQ35542160-38BC40BA-6910-483E-A9C1-99ACC4DE5F24Q35705578-442E4A92-CA7E-490B-A919-60A4A4362154Q35783405-D3F80C02-40AA-4AD9-9AA1-E5BC12EA6E53Q35797626-3F6BF8E5-267F-421C-BD20-3033FE978528Q35939135-DACA87FD-F1D8-4082-8FAF-6C65849B0699Q35957752-42CF6B2B-849A-4A5B-AC6D-CA2625720988Q36066451-958142F5-641C-4F30-9E9F-4F7237EB07BDQ36238311-915587E6-9A65-44CC-84D6-412A23049CF5Q36252073-EFF6CA18-865D-47DF-9B5F-AA24D4D3991CQ36256752-E2C1FADC-25D9-461A-9AE8-860424C271FDQ36354305-BB9CE6C8-7FCE-4848-90CB-C8B5DF0ED799Q36453504-B8447439-4F5A-4CC2-8ED2-F26F900F703DQ36715345-7EAB9DFB-490C-414F-850A-4D83A4752344Q36858391-68949F55-4952-48F0-ACF5-90E92C4A2124Q37259916-EDAE6DF2-BBF6-4F07-880E-189320E59774Q37622767-EB3A0D0E-5602-4E4B-B169-1B8B1B857B37Q37785523-45F186E1-5B96-451A-A7A6-895B0C049B57Q38118462-9452884E-B605-46B6-9B0E-599D513AFE90Q38161285-A76D11CC-9656-4E3E-8B1A-A5AEBA169F3FQ38470842-44497C78-C718-482E-9363-3168E2251902Q39078181-5103AC86-62D2-44AB-AE7E-A523DE4CF0B5Q40298305-058727D9-CE64-450A-B6AE-D6D271846251Q40304033-FCC23CAD-9B70-4615-9459-E92C39DC5CA4Q40321445-E5AAA315-B191-45ED-A7FC-483961CFF7BB
P50
description
German experimental biophysicist and university lecturer
@en
academisch docent
@nl
deutscher experimenteller Biophysiker und Hochschullehrer
@de
name
Joachim Heberle
@af
Joachim Heberle
@an
Joachim Heberle
@ast
Joachim Heberle
@bar
Joachim Heberle
@br
Joachim Heberle
@ca
Joachim Heberle
@co
Joachim Heberle
@cs
Joachim Heberle
@cy
Joachim Heberle
@da
type
label
Joachim Heberle
@af
Joachim Heberle
@an
Joachim Heberle
@ast
Joachim Heberle
@bar
Joachim Heberle
@br
Joachim Heberle
@ca
Joachim Heberle
@co
Joachim Heberle
@cs
Joachim Heberle
@cy
Joachim Heberle
@da
prefLabel
Joachim Heberle
@af
Joachim Heberle
@an
Joachim Heberle
@ast
Joachim Heberle
@bar
Joachim Heberle
@br
Joachim Heberle
@ca
Joachim Heberle
@co
Joachim Heberle
@cs
Joachim Heberle
@cy
Joachim Heberle
@da
P214
P227
P1053
D-8605-2016
P106
P19
P21
P214
P227
P31
P3829
P496
0000-0001-6321-2615
P569
1960-10-01T00:00:00Z
P734
P735
P7859
viaf-241630922