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Variable temperature unit

Manufactured by Bruker

The variable-temperature unit is a piece of lab equipment designed to precisely control the temperature of a sample during analysis or experimentation. It provides a stable and adjustable temperature environment to facilitate a range of applications within the laboratory setting.

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4 protocols using variable temperature unit

1

Solid-state NMR of Labeled Peptides

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All ssNMR spectra were recorded on a 9.4 Tesla Bruker Avance I NMR spectrometer, operating at frequencies of 400 MHz (1H) and 100 MHz (13C). Magic angle spinning (MAS) frequency was 10 kHz for all experiments.
Labelled peptides were packed into kevlar inserts (Bruker) which in turn fit into standard zirconia 4 mm rotors (Bruker).
13C and 15N cross polarization (13C CP) experiments: The standard CP sequence in the Bruker pulse program library was used with 1H 90° pulse length 2.5 μs, contact time 2.5 ms; during the contact pulse a ramped pulse was applied on 1H with average spin lock field of 70 kHz. During acquisition, SPINAL64 decoupling at field strength 100 kHz was applied on 1H. Chemical shifts were referenced to external glycine (α polymorph), using the methylene signal at 43.1 ppm relative to TMS (13C).
Variable temperature experiment: using a Bruker Variable Temperature Unit, the temperature of the sample was varied from 242 K to 342 K in steps of 5 K. At each temperature, the sample was allowed to equilibrate for up to 10 minutes before a standard 13C CP-MAS spectrum was recorded.
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2

EPR Spectroscopy of Radical-Labeled Compounds

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Electronic paramagnetic
resonance spectroscopy (EPR) spectra were
obtained with an X-Band (9.7 GHz) Bruker ELEXSYS 500 spectrometer
equipped with a ST8911 microwave cavity, a Bruker variable-temperature
unit, a field frequency lock system Bruker ER 033 M and equipped with
an NMR Gaussmeter Bruker ER 035 M. The modulation amplitude was kept
well below the line width, and the microwave power was well below
saturation. All liquid samples were previously degassed with Ar. A
quantitative EPR study was performed for G3-Tyr-PROXYL-ONa under the
same conditions and at the same concentration as for G0- to G3-Tyr-PROXYL-OLi,28 (link) comparing the corresponding double integration
value of the EPR spectrum with those of the former ones, resulting
in an area matching the full radical substitution. EPR spectra of
urine were carried out in a quartz flat cell, and the different organ
tissues were analyzed using a quartz tissue cell. Previously,
tissue organs were weighed in an analytical balance.
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3

NMR Spectroscopy for Lipid Relaxation

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1H NMR spectra were recorded on a Bruker AVHD-500 (500 MHz) NMR spectrometer (Billerica, MA, USA) with temperature control. Deuterated solvent D2O (99.9% D, Aldrich, St. Louis, MO, USA) was used as-received. Relaxation rate (R2) was estimated using the signal line with in 1D NMR experiments. Analysis of the line shapes was carried out using Fityk software [43 (link)]. Due to the fast exchange between bound and free lipids, the half-width of the signal was associated with the spin–spin relaxation time, T2, through the following ratio:
Temperature control was achieved using a Bruker variable-temperature unit. All experiments were repeated three times.
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4

EPR Characterization of Nickel Azurin

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Continuous-wave X-band EPR measurements
were collected at either 100 K on a Bruker EMXPlus equipped with a
Bruker variable-temperature unit or at 30 K using a liquid helium
cryostat using a Bruker EMX instrument equipped with an Oxford flow
cryostat (ITC-500). An aliquot of CH3I, 13CH3I (Sigma-Aldrich), or CD3I (Sigma-Aldrich) was
rapidly hand-mixed into a septum-capped EPR tube (Wilmad Lab glass,
727-SQ-250MM) containing 300 μM M121A NiIAz to a
final concentration of 1.5 mM and quenched at varying time points
in a liquid nitrogen-isopentane bath held at approximately 150 K.
Spectra were collected at 30 K with a modulation frequency of 100
kHz and a modulation amplitude of 10 G at a power of 0.2 mW using
30 dB attenuation. For high-resolution spectra at 100 K, a modulation
amplitude of 1 G was used, and data points were collected every 0.1
G with a time constant of 10.24 ms and a conversion time of 40 ms.
Photolysis studies employed the use of a white LED light (Luxeon).
A power saturation study of the trapped intermediate was collected
at 5 K at the Ohio Advanced EPR Facility at Miami University. Spectra
were baseline-corrected by subtraction of a spline using Igor Pro
(Wavemetrics, Lake Oswego, OR) data analysis software. The baseline-corrected
EPR spectra were simulated with the EasySpin toolbox76 (link) within MATLAB.
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