Hello!
I'm working on a molecular ion peak mass spec problem and I'm a bit confused. I thought this would have a peak at 242, a peak twice as intense at 244, and a peak as intense as the first at 246 (1:2:1 ratio). When I looked up pictures of the mass spec to confirm this, I found they had peaks at 163 and 165? I'm just a bit confused on why you wouldn't add it all up including all of the possibilities for combos of the two bromine isotopes. Thank you!
Compound solely composed of C,F & B. It is 42.3% C and 55.66% F by mass. A 2.251g sample of the compound is dissolved in 347.0ml of solution produces a 0.01267M solution. What is the molecular formula of the compound.
I get to the ratio part but the numbers aren't whole number so I don't know how to find the empirical formula first?
I really don't get it. I just assume verything as molar mass.
Or do the connections between molecules not get affected by the acceleration?
I was doing some ideal gas law and relative molecular mass questions but I was unsure about the units. Using the density formula, I got to M (around 0.00641) but I was unsure about the units. I knew I had to multiply by 1000 to get to g mol^-1 but what are the units before you multiply by 1000?
If Mars had water with rivers and lakes and all that stuff, what happened to all of it and its molecular mass that came with it?
I assume water has a high enough mass that it wouldnt all just evaporate away with no signs of it anywhere.
So what happen to it?
I created a coded Mr calculator and I wondered if that'd be the sort of thing that would be useful to people?
I have a parent ion of 114 which is also the molecular weight from what I understand. Using the rule of 13 I get the molecular formulas:
C8H18, C7H14O, C6H10O2, C5H6O3, C4H2O4.
Using the degree of unsaturation formula: U=C+1=1/2(H-N)
U=8+1=(1/2)(18-0)
U=9
Did I do this correctly? And should I have tried molecular formulas using N instead or alongside O?
Bet I’ll get CENSORED for this.
Keeping count: Reported is the quantification of protein–protein interactions with light using mass photometry, which detects, images, and quantifies light scattering of single proteins upon binding to an illuminated glass‐water interface. The resulting signals are proportional to the molecular mass of each species and overall abundance, providing a new means to measure the relative abundances of proteins and their complexes, thereby enabling measurement of binding affinities and kinetics by molecular counting.
Abstract
Interactions between biomolecules control the processes of life in health and their malfunction in disease, making their characterization and quantification essential. Immobilization‐ and label‐free analytical techniques are desirable because of their simplicity and minimal invasiveness, but they struggle with quantifying tight interactions. Here, we show that mass photometry can accurately count, distinguish by molecular mass, and thereby reveal the relative abundances of different unlabelled biomolecules and their complexes in mixtures at the single‐molecule level. These measurements determine binding affinities over four orders of magnitude at equilibrium for both simple and complex stoichiometries within minutes, as well as the associated kinetics. These results introduce mass photometry as a rapid, simple and label‐free method for studying sub‐micromolar binding affinities, with potential for extension towards a universal approach for characterizing complex biomolecular interactions.
https://ift.tt/3cVRRr4
Some websites says they are same
Are they the same thing??? If not, what's the difference?
