scholarly journals Real-time NMR spectroscopy in the study of biomolecular kinetics and dynamics

2021 ◽  
Author(s):  
György Pintér ◽  
Katharina F. Hohmann ◽  
J. Tassilo Grün ◽  
Julia Wirmer-Bartoschek ◽  
Clemens Glaubitz ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Nuclear Polarization ◽  
Signal To Noise ◽  
Nmr Studies ◽  
Equilibrium Conditions ◽  
Time Resolved ◽  
Kinetics And Dynamics ◽  
Time Limitations ◽  
Kinetics Of ◽  
Rna And Dna

Abstract. The review describes the application of NMR spectroscopy to study kinetics of folding, refolding and aggregation of proteins, RNA and DNA. Time-resolved NMR experiments can be conducted in a reversible or an irreversible manner. In particular irreversible folding experiments pose large requirements on (i) the signal-to-noise due to the time limitations and (ii) on synchronizing the refolding steps. Thus, this contribution discusses the application of methods for signal-to-noise increases including dynamic nuclear polarization, hyperpolarization and photo-CIDNP for the study of time-resolved NMR studies. Further, methods are reviewed ranging from pressure- and temperature-jump, light induction and rapid mixing to induce rapidly non-equilibrium conditions required to initiate folding.

scholarly journals Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics

2021 ◽  
Vol 2 (1) ◽  
pp. 291-320
Author(s):  
György Pintér ◽  
Katharina F. Hohmann ◽  
J. Tassilo Grün ◽  
Julia Wirmer-Bartoschek ◽  
Clemens Glaubitz ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Resonance Spectroscopy ◽  
Signal To Noise ◽  
Nmr Studies ◽  
Time Resolved ◽  
Kinetics And Dynamics ◽  
Time Limitations ◽  
Kinetics Of ◽  
Nuclear Magnetic

Abstract. The review describes the application of nuclear magnetic resonance (NMR) spectroscopy to study kinetics of folding, refolding and aggregation of proteins, RNA and DNA. Time-resolved NMR experiments can be conducted in a reversible or an irreversible manner. In particular, irreversible folding experiments pose large requirements for (i) signal-to-noise due to the time limitations and (ii) synchronising of the refolding steps. Thus, this contribution discusses the application of methods for signal-to-noise increases, including dynamic nuclear polarisation, hyperpolarisation and photo-CIDNP for the study of time-resolved NMR studies. Further, methods are reviewed ranging from pressure and temperature jump, light induction to rapid mixing to induce rapidly non-equilibrium conditions required to initiate folding.

Kinetic Evidence for Transiently Shifted Acidity Constant of Histidine Linked to Paramagnetic Tyrosine Probed by Intramolecular Electron Transfer in Oxidized Peptides

2021 ◽  
Author(s):  
Olga B. Morozova ◽  
Dmitri Stass ◽  
Alexandra V. Yurkovskaya
Keyword(s):  
Electron Transfer ◽  
Dynamic Nuclear Polarization ◽  
Nuclear Polarization ◽  
Intramolecular Electron Transfer ◽  
Acidity Constant ◽  
Time Resolved ◽  
Chemically Induced ◽  
Kinetics Of

Kinetics of electron transfer (ET) from tyrosine (Tyr) to short-lived histidine (His) radicals in peptides of different structures was monitored using time-resolved chemically induced dynamic nuclear polarization (CIDNP) to follow...

scholarly journals Sub-minute kinetics of human red cell fumarase:1H spin-echo NMR spectroscopy and13C rapid-dissolution dynamic nuclear polarization

2018 ◽  
Vol 31 (3) ◽  
pp. e3870 ◽  
Author(s):  
Dmitry Shishmarev ◽  
Alan J. Wright ◽  
Tiago B. Rodrigues ◽  
Giuseppe Pileio ◽  
Gabriele Stevanato ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Dynamic Nuclear Polarization ◽  
Nuclear Polarization ◽  
Spin Echo ◽  
Red Cell ◽  
Rapid Dissolution ◽  
Kinetics Of ◽  
Dissolution Dynamic Nuclear Polarization

Intramolecular Electron Transfer from Tryptophan to Guanosyl Radicals in a Linked System as a Model of DNA Repair

2017 ◽  
Vol 231 (3) ◽  
Author(s):  
Olga B. Morozova ◽  
Natalya N. Fishman ◽  
Alexandra V. Yurkovskaya
Keyword(s):  
Electron Transfer ◽  
Dna Repair ◽  
Kinetic Data ◽  
Nuclear Polarization ◽  
Intramolecular Electron Transfer ◽  
Time Resolved ◽  
Purine Base ◽  
Chemically Induced ◽  
Kinetics Of

AbstractAs a model of chemical DNA repair, intramolecular electron transfer from tryptophan to the radical of the purine base guanosine combined into a conjugate by a flexible linker was studied by time-resolved chemically induced dynamic nuclear polarization (CIDNP). The guanosyl radicals were photochemically generated in the quenching reaction of the triplet excited dye 2,2′-dipyridyl. The CIDNP kinetics was obtained by detection of NMR spectra containing anomalously enhanced signals of diamagnetic products that are formed during a variable period after excitation by a laser pulse. The kinetic data obtained for the protons located on the guanosyl and tryptophanyl moieties of the conjugate were compared to those obtained in photoreactions of the molecules containing the same linker, but with only one of the two reactive moieties of the conjugate – tryptophanyl or guanosyl. Strong differences between the CIDNP kinetics of different conjugates were revealed and explained by a rapid intramolecular electron transfer from tryptophan to the guanosyl radical in the conjugate. Model simulations of the CIDNP kinetics allowed for determination of the rate constant of intramolecular electron transfer at (1.0±0.5)×10

In situ Time-Resolved Small-Angle X-ray Scattering Reveals the Formation Kinetics of Polyelectrolyte Complex Micelles

2019 ◽  
Author(s):  
Hao Wu ◽  
Jeffrey Ting ◽  
Siqi Meng ◽  
Matthew Tirrell
Keyword(s):  
Small Angle ◽  
Self Assembly ◽  
Electrostatic Interactions ◽  
Polyelectrolyte Complex ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Kinetics Of ◽  
Ray Scattering

We have directly observed the <i>in situ</i> self-assembly kinetics of polyelectrolyte complex (PEC) micelles by synchrotron time-resolved small-angle X-ray scattering, equipped with a stopped-flow device that provides millisecond temporal resolution. This work has elucidated one general kinetic pathway for the process of PEC micelle formation, which provides useful physical insights for increasing our fundamental understanding of complexation and self-assembly dynamics driven by electrostatic interactions that occur on ultrafast timescales.

Sign in / Sign up

Export Citation Format

Share Document