Opus 6.5 analysis software

Manufactured by Bruker

Sourced in United States

OPUS 6.5 is a spectroscopy analysis software developed by Bruker. It provides a platform for data acquisition, processing, and analysis of spectroscopic measurements. The software is compatible with a range of Bruker spectrometers and supports various spectroscopic techniques, including infrared, Raman, and nuclear magnetic resonance.

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Lab products found in correlation

Nicolet nexus spectrometer, by Thermo Fisher Scientific (5 mentions) Smart itr accessory, by Thermo Fisher Scientific (2 mentions)

Close spelling variants of this product

OPUS software (229 citations) OPUS 6.5 software (86 citations) OPUS 5.5 software (27 citations)

5 protocols using opus 6.5 analysis software

Solid-state FTIR Characterization

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ssFTIR measurements were conducted in attenuated total reflectance mode using a Nicolet Nexus spectrometer (Thermo Scientific, Waltham, MA) equipped with a Smart iTR accessory. Powders were loaded and compressed against the diamond by a metal anvil. The spectra were collected in the absorbance mode in the range of 800 to 4000 cm⁻¹, with 120 scans and 4 cm⁻¹ resolution. Using OPUS 6.5 analysis software (Bruker, Billerica, MA), the results were processed using baseline correction, smoothing, normalization, and second derivatization.

Wilson N.E., Topp E.M, & Zhou Q.T. (2019). Effects of Drying Method and Excipient on Structure and Stability of Protein Solids Using Solid-State Hydrogen/Deuterium Exchange Mass Spectrometry (ssHDX-MS). International journal of pharmaceutics, 567, 118470.

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Protein Secondary Structure Analysis via ATR-FTIR

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Attenuated total reflectance (ATR) mode on a Nicolet Nexus spectrometer (Thermo Scientific, Waltham, MA, USA) equipped with Smart iTR accessory was used to obtain the ssFTIR spectra for the protein secondary structural analysis. A range of 800 to 4000 cm⁻¹ in absorbance mode at 4 cm⁻¹ resolution was used to collect the data. All spectra were corrected for moisture content and CO₂. OPUS 6.5 analysis software (Bruker, Billerica, MA, USA) was used to process the spectra with baseline correction, smoothing, normalization, and second derivatization.

Mutukuri T.T., Ling J., Du Y., Su Y, & Zhou Q.(. (2022). Effect of buffer salts on physical stability of lyophilized and spray-dried protein formulations containing bovine serum albumin and trehalose. Pharmaceutical research, 40(6), 1355-1371.

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Attenuated Total Reflectance FTIR Analysis

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Measurements were conducted with a Thermo Scientific Nicolet Nexus spectrometer (Waltham, MA) in the attenuated total reflectance mode. Samples were loaded onto a Smart iTR™ accessory and compressed against the diamond by a metal anvil. Spectra were collected in absorbance mode with 120 scans in the range of 800 to 4000 cm⁻¹ with a 4 cm⁻¹ resolution. Results were processed with OPUS 6.5 analysis software (Bruker, Billerica, MA) using baseline correction, smoothing, normalization, and second derivatization.

Wilson N.E., Mutukuri T.T., Zemlyanov D.Y., Taylor L.S., Topp E.M, & Zhou Q.(. (2019). Surface Composition and Formulation Heterogeneity of Protein Solids Produced by Spray Drying. Pharmaceutical research, 37(1), 14.

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Protein Secondary Structure Analysis by FTIR

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Attenuated total reflectance (ATR) mode on a Nicolet Nexus spectrometer (Thermo Scientific, Waltham, MA, USA) equipped with Smart iTR accessory was used to obtain the ssFTIR measurements for the protein secondary structural analysis. A range of 800 to 4000 cm⁻¹ in absorbance mode at 4 cm⁻¹ resolution was used to collect the data. All spectra were corrected for moisture content and CO₂. OPUS 6.5 analysis software (Bruker, Billerica, MA, USA) was used to process the spectra with baseline correction, smoothing, normalization, and second derivatization.

Mutukuri T.T., Maa Y.F., Gikanga B., Sakhnovsky R, & Zhou Q.(. (2021). Electrostatic Spray Drying for Monoclonal Antibody Formulation. International journal of pharmaceutics, 607, 120942.

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Protein Secondary Structure Characterization by ATR-FTIR

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A Nicolet Nexus spectrometer (Thermo Scientific, Waltham, MA) equipped with Smart iTR accessory was used in attenuated total reflectance (ATR) mode to conduct the ssFTIR measurements for secondary structural analysis. After the samples were loaded and compressed against the diamond, spectra were collected in the range of 800 to 4000 cm⁻¹ in absorbance mode with co-addition of 120 scans obtained at 4 cm⁻¹ resolution. The resulting spectra were processed using OPUS 6.5 analysis software (Bruker, Billerica, MA) with baseline correction, smoothing, normalization and second derivatization.

Mutukuri T.T., Wilson N.E., Taylor L.S., Topp E.M, & Zhou Q.T. (2020). Effects of Drying Method and Excipient on the Structure and Physical Stability of Protein Solids: Freeze Drying vs. Spray Freeze Drying. International journal of pharmaceutics, 594, 120169.

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