What is the Redox Potential of my neurotransmitters?

If they are equivalent, does the entropy calculated using the Shannon formula follow the law of entropy increase for macroscopic physical processes? If not, what is the difference between them?

how many bands does BSA give in sds page?

I need to purify proteins with HisTag by means of beads fused with NTA. The proteins are in a buffer containing DMSO. After purification no proteins bind the beads, they are in the unbound fraction.

Can DMSO affect the interaction of the HisTag with the NTA-beads?

Does the DNA remain stable or degrade at this temperature? Would there be any difference in thermal stability between supercoiled and linear forms of say, 3 kb plasmid.

Most people say that imidazole doesnt affect the majority of downstream applications for purified proteins but it is a chelator, so you would think that it might chelate the Mg2+ in solution and inhibit Mg2+ dependent reactions. Anyone seen any papers that discuss what concentration Imidazole will chelate magnesium or manganese ions in solution?

Dear,

I am working on cell cultures and labeling nascent translated proteins with methionine analog - AHA. Then I perform "click reaction" on cell lysates to tag freshly translated proteins with biotin. Can anyone advise me on what type of magnetic dynabeads is best for pulling down full AHA-biotin labeled proteins? I have successfully used M-270 dynabeads to pull down tryptic AHA-biotin labeled peptides but for full proteins I have good enrichment only for small <35 kDa proteins. Are some other dynabeads like C1 streptavidin better for full proteins? What can I do and what types of beads are best for pull-down of larger proteins. All suggestions and advice are welcome.

Dear colleagues,

I am extracting a genomic DNA for sequencing with nanopore, and therefore am very cautious about quality checks. Recently I eluted the same DNA sample from a purification column with water and with elution buffer (EB), because, apparently, water leaves half of the DNA on the column, so I added EB to be sure that I got it all.

Next, nanodrop ratios were good for water solution but for the DNA in EB 260/230 ratio was 8. I did blank against the buffer, when measuring it.

What can be the reason and should I worry about the quality of my DNA in EB?

The EB was supplied with the column an is standard Tris-EDTA (DNA clean&concentrator kit from Zymoresearch).

Looking forward to your advice!

I was checking Ag-Ab interaction using biosensor (APS)and then I got a association dissociation curve that increasing at both steps and so I need to explain that if there is available reason.