nice to learn about these "wet" lab things as well, thanks! wondering what are the downstream impact on LC MS MS IDs? Is there an review article on what kinds and amounts of proteins one gets with different reagents and workflows in general?

Great video🫢

This is SUCH. A. GOOD. VIDEO!

The lecture was incredibly informative and clear.

Physical Biochem exam today, you are a saviour dude :D

HOW DID YOU IDENTIFIED THESE ARE ISOTOPES OF CARBON

Super great! Thank you very much. It is very helpful to me, a beginner of MS user

like and subscribed 👍

I have a "chicken or egg" type question! where does the uniprot database come from? if it is the mass spectrometer that gives the sequence information, does the uniprot database derive from mass spec data? I also have another question; is uniprot different from a spectral library database for data independent acquisitions?

Thank you so much! I needed this for my uni course.

Great video, really nice and understandable introduction.

This was very helpful but I still have one question. I don't get why the relative intensities of complementary b and y fragments are different, like b2 and y10 in your example. I mean, when the parent ion fragments on a specific bond you get the same amount of the two complementary fragments, so I really don't get this. could you help me please?

Thanks a lot for these videos. However, a doubt remains. The peptic fragments are just being blasted with inert gas to break them down into b and y ions. Where from are the extra 1 or rather 2 H+ at the N terminal of 'y-ions' coming from, giving them overall +1 charge?

Bloody legend mate

This guy is extremely good, super kind.. it is such a huge sacrifice to be able to dispense such finer details to the seekers of this knowledge. I am so grateful to you, Sir. I wish you good health and long life and a happy family and a tranquil working atmosphere wherever you are; you are a great treasure to me and many more. You are the best I have ever encountered here.

You're a legend! This is currently helping me with my mass spec lab in my biochemistry degree 💪🏽📊

Hi, where can I find the original figure you use at 3:02?

Hi, thanks for the great lecture series. Could you share the link to the interactive learning module for ETD at 27:20?

Hey sir! Thanks for the help- question I had is how would you draw a simple mechanism for the y and b fragmentation? How do both the nitrogen np oxygen become positively charged? Thanks for the vid!

Thank you so much, I definitely owe you one 👏🙌

I have a questions I did all this, b ions I got sequence of RYAAYKYA and for y ions I have the sequence of IKAYKYAA I am not sure what's my final sequence going to be

Very easy to follow along and clear overall material presented in the video. Thank you very much, it is a pleasure to learn with you explaining these novel to me concepts.

Excellent video, thanks very much!

brilliant lecture! thank you so much!

Can you please name that 2010 paper?

The Thermo video (kzfaq.info/get/bejne/gdCFhLym3pnRo5U.html) is no longer available.

Hello, thank you for the video, I learned a lot. but in kzfaq.info/get/bejne/gpx9e7aTnK-cYmQ.html , the reason that the second peak is not for an amino acid is that its difference from the first peak is 61 and it is between the mass of Gly (57) and Ala (71), however, you said that its difference is less than 57.

I wonder how you know if you need to subtract a water molecule or not from the fragment.

Best explanation I saw. Congrats!

Which software you have used for matching the fragment ion of peptide?

Thanku

pls share the Karen Jhon Shaw link

Helping a ton for my proteomics course final! Thanks!!

This was very helpful! Thank you!

Could you pls sometime, if possible, run a sample and optimize the Mass Spectrometry conditions. Basically develop a method. That would be the best.

Is there a resource preferably videos for beginners to learn exhaustively.

Thanks Matthew for this very nice and comprehensive lecture series. I learned a lot. It would be great if you could paste the links to other sources that you mentioned in your videos down in the description. This makes it easier to access the other videos.

Really enjoying your videos! Thank you for uploading these; such high quality lectures and slides.

This is a really good lecture. Thank you very much!

You are such a life-saver! I am doing the final thesis for my master course and I am having the worst tutor/mentor ever. It is too late and too risky for me to change the mentor now. Your videos really help me a lot. Hope that in a year, I can have everything sorted out.

Great...

Do you do shotgun proteomics? If so can I ask you a few questions about the instruments for this purpose?

From the two instruments, you showed at the beginning (Q Exactive Plus and Synapt XS), which one is better for shotgun proteomics? (The type of proteomics when you want to identify as many proteins as possible from a sample...)

A comprehensive overview of Mass spectrometry. Good job Matthew.

your explanatory videos are ultra helpful! I am a masters student in biochemistry lab and these now form the basis of my understanding of MS. I have a question however: Why do we subtract another 18 amu (a H2O molecule) from the intact peptide in addition to the largest b ion in order to determine the first (and why only the first?) aa from the carboxyl-terminal (lys/arg), as in: intact - b3 - 18 = lys/arg ? instead of: intact + 18 = b3 + lys/arg => intact + 18 - b3 = lys/arg ? Aren't we referring to the water molecule that breaks the peptide bond between b3 and lys/arg or am I missing something ?

Specta is plural. One is a mass spectrum.

thanks so much

thanks for sharing bro

This is absolutely AMAZING. Thank you and please make more videos science needs you.

Thank you very much! Very clear explanation!