The largest database of trusted experimental protocols

1 mm high precision quartz cell

Manufactured by Hellma
Sourced in United Kingdom

The 1 mm high precision quartz cell is a specialized laboratory equipment designed for precise optical measurements. It features a 1 mm path length and is made of high-quality quartz material. This cell is intended for use in various analytical techniques that require accurate optical path lengths and sample containment.

Automatically generated - may contain errors

Lab products found in correlation

7 protocols using 1 mm high precision quartz cell

1

CD Spectroscopy of Phylloseptin Peptides

Check if the same lab product or an alternative is used in the 5 most similar protocols
CD spectra were obtained at 20 °C using a 1 mm high precision quartz cell (Hellma Analytics, Essex, UK) with a JASCO J-815 CD spectrometer (Jasco, Essex, UK). The measurement range was from 250 nm to 190 nm at a scanning speed of 200 nm/min. The bandwidth was 1 nm, and the data pitch was 0.5 nm. Phylloseptin-PTa and phylloseptin-PHa were respectively dissolved in 10 mM NH4Ac or 10 mM NH4Ac with 50% TFE to reach a final concentration of 100 μM. The experimental data were processed via DICHROWEB [35 (link),36 (link),37 (link)] and the α-helicity was calculated by K2D analysis programme [38 (link)].
+ Open protocol
+ Expand
2

Peptide Secondary Structure Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
The secondary structure of the peptide was determined using a JASCO J-815 CD spectrometer (Jasco, Essex, UK). It was dissolved in 10 mM ammonium acetate and 10 mM ammonium acetate with 50% trifluoroethanol (TFE), respectively and then was prepared at 100 µM in a 1 mm high precision quartz cell (Hellma Analytics, Essex, UK). CD spectra were recorded at a wavelength ranging from 190 nm to 250 nm with a 100 nm/min scan speed. The parameters were set as 1 nm bandwidth and 0.5 nm data pitch.
We supplemented the secondary structure prediction with some bioinformatics tools. A vividly visual plot containing some further details about alpha helices was demonstrated by helical wheel projections. The significant properties of the novel peptide were predicted by Heliquest (http://heliquest.ipmc.cnrs.fr/cgi-bin/ComputParams.py). Additionally, the I-TASSER webserver [37 (link),38 (link)] was utilized to simulate a 3D model. Overall qualities of the predicted model were evaluated by z-scores using ProSA [39 (link),40 (link)].
+ Open protocol
+ Expand
3

Circular Dichroism Analysis of Peptides

Check if the same lab product or an alternative is used in the 5 most similar protocols
The sample peptide solutions (50 μM) were prepared in a 1 mm high precision quartz cell (Hellma Analytics, Essex, UK) by 10 mM ammonium acetate and 50% TFE in 10 mM ammonium acetate buffer respectively. CD measurements were performed at room temperature by a JASCO J-815 CD spectrometer (Jasco, Essex, UK) across the wavelength range from 190 nm-260 nm. The scanning speed was 100 nm/min, the bandwidth was 1 nm and the data pitch was 0.5 nm. The CD spectra were further analysed using the online software, BeStSel35 (link), and the following proportion of different secondary structures were predicted.
+ Open protocol
+ Expand
4

Circular Dichroism Analysis of Peptides

Check if the same lab product or an alternative is used in the 5 most similar protocols
A JASCO J-815 CD spectrometer (Jasco, Essex, UK) was employed to perform the analysis of peptide secondary structures. Each peptide was dissolved in 10 mM ammonium acetate and 10 mM ammonium acetate with 50% TFE, respectively, to reach a concentration of 100 μM, in a 1 mm high precision quartz cell (Hellma Analytics, Essex, UK). All CD spectra were obtained at 20 °C from 250 nm to 190 nm at a scanning speed of 100 nm/min. The bandwidth was 1 nm, and the data pitch was 0.5 nm. K2D3 webserver [19 (link)] was used to estimate the α-helix content of the peptides from their CD spectrum data.
+ Open protocol
+ Expand
5

Circular Dichroism Analysis of Peptides

Check if the same lab product or an alternative is used in the 5 most similar protocols
The sample peptide solutions (50 μM) were prepared in a 1 mm high precision quartz cell (Hellma Analytics, Essex, UK) with 10 mM ammonium acetate and 50% TFE in 10 mM ammonium acetate buffer respectively. CD measurements were performed at 20 °C by a JASCO J-815 CD spectrometer (Jasco, Essex, UK) across the wavelength range of 190–250 nm. The scanning speed was 100 nm/min, the bandwidth was one nm, and the data pitch was 0.5 nm. The CD spectra were further analysed using the online software, BeStSel [23 (link)], and the proportion of different secondary structures were predicted.
+ Open protocol
+ Expand
6

Structural Characterization of Antimicrobial Peptides

Check if the same lab product or an alternative is used in the 5 most similar protocols
The secondary structure of each peptide was determined using a JASCO J-815 CD spectrometer (Jasco, Essex, UK). Each peptide was dissolved in 10 mM ammonium acetate and 10 mM ammonium acetate with 50% TFE, respectively and was prepared at 100 μM in a 1 mm high precision quartz cell (Hellma Analytics, Essex, UK). CD spectra were recorded at a wavelength ranging from 190 nm to 250 nm with a 100 nm/min scan speed. The parameters were set as 1 nm bandwidth and 0.5 nm data pitch. The result was analysed by the K2D3 webserver to estimate α-helical content [24 (link)]. The helical wheel projections and significant physiochemical parameters of peptides, were predicted by use of Network Protein Sequence Analysis [25 ] and Heliquest [26 ] programmes. The helical wheel projection was utilized to describe the properties of alpha helices as a visual plot [27 ]. The significant parameters such as hydrophobicity, hydrophobic moment, and net charge at neutral pH, which were considered as significant factors correlating with antimicrobial activity, antimicrobial spectrum, and haemolysis, were also predicted and calculated [28 (link),29 (link),30 (link),31 (link),32 ].
+ Open protocol
+ Expand
7

Circular Dichroism Spectroscopy of Peptides

Check if the same lab product or an alternative is used in the 5 most similar protocols
The sample peptide solutions (50 μM) were prepared in 10 mM ammonium acetate initially in a 1 mm high precision quartz cell (Hellma Analytics, Essex, UK). CD measurements were performed at room temperature by a JASCO J-815 CD spectrometer (Jasco, Essex, UK) across the wavelength range from 190 nm-250 nm. The scanning speed was 100 nm/min, the bandwidth was 1 nm and the data pitch was 0.5 nm.
+ Open protocol
+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Sign up for free.
Registration takes 20 seconds.
Available from any computer
No download required

Sign up now

Revolutionizing how scientists
search and build protocols!