Infrared difference spectroscopy of proteins: from bands to bonds
VA Lorenz-Fonfria - Chemical reviews, 2020 - ACS Publications
Infrared difference spectroscopy probes vibrational changes of proteins upon their
perturbation. Compared with other spectroscopic methods, it stands out by its sensitivity to …
perturbation. Compared with other spectroscopic methods, it stands out by its sensitivity to …
Breaking barriers in ultrafast spectroscopy and imaging using 100 kHz amplified Yb-laser systems
PM Donaldson, GM Greetham… - Accounts of Chemical …, 2023 - ACS Publications
Conspectus Ultrafast spectroscopy and imaging have become tools utilized by a broad
range of scientists involved in materials, energy, biological, and chemical sciences …
range of scientists involved in materials, energy, biological, and chemical sciences …
Optical control of ultrafast structural dynamics in a fluorescent protein
The photoisomerization reaction of a fluorescent protein chromophore occurs on the ultrafast
timescale. The structural dynamics that result from femtosecond optical excitation have …
timescale. The structural dynamics that result from femtosecond optical excitation have …
Map** the complete photocycle that powers a large Stokes shift red fluorescent protein
Large Stokes shift (LSS) red fluorescent proteins (RFPs) are highly desirable for bioimaging
advances. The RFP mKeima, with coexisting cis‐and trans‐isomers, holds significance as …
advances. The RFP mKeima, with coexisting cis‐and trans‐isomers, holds significance as …
Iminothioindoxyl as a molecular photoswitch with 100 nm band separation in the visible range
Light is an exceptional external stimulus for establishing precise control over the properties
and functions of chemical and biological systems, which is enabled through the use of …
and functions of chemical and biological systems, which is enabled through the use of …
Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy
J Woodhouse, G Nass Kovacs, N Coquelle… - Nature …, 2020 - nature.com
Reversibly switchable fluorescent proteins (RSFPs) serve as markers in advanced
fluorescence imaging. Photoswitching from a non-fluorescent off-state to a fluorescent on …
fluorescence imaging. Photoswitching from a non-fluorescent off-state to a fluorescent on …
Large Stokes shift fluorescence activation in an RNA aptamer by intermolecular proton transfer to guanine
M Mieczkowski, C Steinmetzger, I Bessi… - Nature …, 2021 - nature.com
Fluorogenic RNA aptamers are synthetic functional RNAs that specifically bind and activate
conditional fluorophores. The Chili RNA aptamer mimics large Stokes shift fluorescent …
conditional fluorophores. The Chili RNA aptamer mimics large Stokes shift fluorescent …
A guide to time‐resolved structural analysis of light‐activated proteins
Dynamical changes in protein structures are essential for protein function and occur over
femtoseconds to seconds timescales. X‐ray free electron lasers have facilitated …
femtoseconds to seconds timescales. X‐ray free electron lasers have facilitated …
Structural characterization of fluorescent proteins using tunable femtosecond stimulated Raman spectroscopy
The versatile functions of fluorescent proteins (FPs) as fluorescence biomarkers depend on
their intrinsic chromophores interacting with the protein environment. Besides X-ray …
their intrinsic chromophores interacting with the protein environment. Besides X-ray …
Protein assembly: Controllable design strategies and applications in biology
Y Li, R Tian, H Shi, J Xu, T Wang, J Liu - Aggregate, 2023 - Wiley Online Library
Protein assembly is the structural basis for the collaboration between proteins to accomplish
life activities due to its realization of the domain‐limited and precise spatial arrangement of …
life activities due to its realization of the domain‐limited and precise spatial arrangement of …