Patrick E. Konold
VU University Amsterdam
17 Papers
32 Citations
Patrick E. Konold is an academic researcher from VU University Amsterdam. The author has contributed to research in topics: Fluorescence & Thylakoid. The author has an hindex of 8, co-authored 13 publications. Previous affiliations of Patrick E. Konold include National Institute of Standards and Technology & University of Colorado Boulder.
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Papers
Photoactivation Mechanism, Timing of Protein Secondary Structure Dynamics and Carotenoid Translocation in the Orange Carotenoid Protein
Patrick E. Konold,Ivo H. M. van Stokkum,Fernando Muzzopappa,Fernando Muzzopappa,Adjélé Wilson,Adjélé Wilson,Marie Louise Groot,Diana Kirilovsky,Diana Kirilovsky,John T. M. Kennis +9 more
TL;DR: A hereto unidentified carotenoid excited state in OCP is identified, the so-called S* state, which is proposed to play a key role in breaking conserved hydrogen-bond interactions between carotanoid and aromatic amino acids in the binding pocket.
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Confinement in crystal lattice alters entire photocycle pathway of the Photoactive Yellow Protein.
Patrick E. Konold,Enis Arik,Jörn Weißenborn,Jos C. Arents,Klaas J. Hellingwerf,Ivo H. M. van Stokkum,John T. M. Kennis,Marie Louise Groot +7 more
TL;DR: It is found that the photocycle kinetics and structural intermediates of PYP deviate in the crystalline state, which must be taken into consideration when planning TRC experiments, illustrates that ultrafast TRC results cannot be uncritically extrapolated to in vivo function and that comparative spectroscopic experiments on proteins in crystalline and solution states can help identify structural intermediate under native conditions.
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Hydrogen bond flexibility correlates with Stokes shift in mPlum variants.
TL;DR: This dynamic model underscores the role of environmental flexibility in the mechanism of excited state solvation and provides a template for engineering next-generation red fluorescent proteins.
The molecular pH-response mechanism of the plant light-stress sensor PsbS.
TL;DR: In this paper, the authors performed an NMR, FTIR and 2DIR spectroscopic analysis of Physcomitrella patens PsbS and of the E176Q mutant in which an active glutamate has been replaced.
Far-Red Emission of mPlum Fluorescent Protein Results from Excited-State Interconversion between Chromophore Hydrogen-Bonding States
TL;DR: It is reported that femtosecond time-resolved area-normalized emission spectra of mPlum show a clear isoemissive point, which can only result from a system with two emitting states, rather than a system that undergoes a continuous spectral red shift, as expected from typical solvation.
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