Endoproteinase Lys-C is a protease that cleaves proteins on the C-terminal side of lysine residues. This enzyme is naturally found in the bacterium Lysobacter enzymogenes and is commonly used in protein sequencing. Lys-C activity is optimal in the pH range 7.0 - 9.0.
== See also ==
Trypsin
== References... ==
Does it have other names? Can I write "Lys-C protease"?
Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction
Preferential cleavage: Lys-, including -Lys-Pro-
This enzyme is isolated from Achromobacter lyticus.
== References ==
== External links ==
Lysyl endopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)...
Are they the same thing?
In my context, this "protease" is used for peptide mapping.
I mean, it's used to digest the protein into small peptides
@CowperKettle By my minuscule knowledge in Biochem, whatever comes before -ase is what's being catalyzed and stuff. So peptidase is for peptides, but protease is for proteins. I guess it differs in some places.
You can only be sure if you know what the two do, exactly.
But usually the same enzymes don't have different names.
@Cowper, endo means that it can cleave peptide bonds within the chain itself.
For example, if you have a polypeptide ABCDEFGHIJ, then an endopeptidase could cut between D and E (for example. Where exactly it cuts will depend on the specificity of the enzyme and its active site).
Whereas an exopeptidase would snip off one amino acid at a time from the ends. So for example it might cut A-B, then B-C...
What is the difference between Endoproteinase Lys-C and Lysyl endopeptidase?
In the text I'm translating about peptide mapping, "lysine protease" is mentioned (in Russian: лизиновая протеаза). This might be erroneous to translate word for word as "lysine protease". There must be a slight error ...
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The Nernst equation does not need a replacement for low concentrations. Yes the limit is $\infty$, which essentially means you can't realistically have zero concentration of anything. We may think of absolutely pure water as an idealized situation. Well, as soon as it gets in touch with copper, s...
Maybe this would be helpful
the energy comes from bonding with water? I'm not sure
So this applies to metal too? Energy is released rather than gained?
?
Every time I ask this question on a forum, they simple reply "You seem to have a lack of understanding of chemistry." and I am like ._., No one actually explained why this occurs
Yea for example, It takes an amount of energy to seprate NaCl then to bond with water it released energy. So if the bonding of water releases more energy that taken to separate NaCl then it becomes exothermic and vice versa
Urea solution is one of the most commonly employed protein denaturants for protease digestion in proteomic studies. However, it has long been recognized that urea solution can cause carbamylation at the N-termini of proteins/peptides and at the side chain amino groups of lysine and arginine residues.
Protein/peptide carbamylation blocks protease digestion and affects protein identification and quantification in mass spectrometry analysis by blocking peptide amino groups from isotopic/isobaric labeling and changing peptide charge states, retention times and masses.
Multitran translates "carbamylation" and "carbamidation" differently.
There's no mention of synonymicity.
If they are synonymous, I'll use the one that is used more often
My authors write that they performed in-gel digestion of the protein, then used MS/MS, then used the NCBI protein database to "piece it together" (my guess)
Pre-experiment stats
Questions
16,753 questions
8,376 without accepted answers
3,460 with no answers
2,830 with no answers and not closed
$\frac{13,923}{16,753} = 83.107\%$
Answers
19,299 answers
Closure
1,641 questions closed
1,124 closed as not a duplicate
517 duplicates
homework
...
@Wildcat I don't see a drastic change either. Some people worried that we'd have a spike in unanswered questions. We haven't had.
@Wildcat We just wanted to see how things go. I'm gonna write a new meta post asking if we should continue being this way or go back to smiting everything that smells.
@Wildcat See how peaceful and rigorously objective meta has become.
No complaints. No rants. No hard feelings. No ragequits.
Nowadays I find more and more of my questions being closed and I don't understand why. I've got the impression that acquiring knowledge isn't the priority here anymore, but rather following some established policies and forms. I think that the homework question policies should be changed. I guess...
@Wildcat I know what I want this site to be. I don't want it to be a homework ghetto. I don't want it to be a clique of only the most elite either. I want those two to coexist without hurting one another.
@pentavalentcarbon Look dude. Some people lie on the heavy moderation part. Some people lie on the let-it-go-as-long-as-long-as-it-doesn't-hurt part. I'm in the middle. I used to be extreme, but I'm in the middle.
@Wildcat Are they now? They've been silenced for the past month as far as I'm aware.
@Wildcat We're not categorizing what we accept or we don't accept. We don't say that if a high school textbook may contain an answer to your question, hidden in some page, you can't ask it here. That's not what we say in the site definition.
Back to the main issue at hand, I still think asking for research is a bit too much.
That, or either you have to lower the bar of what constitutes research to something . . . just not useful.
You have to take askers into account. The minimum acceptable question shouldn't be a bar that high.
And then new, interesting questions will pop up, without demonstrated effort but with potentially good answers.
So you either close them and lose some good discussions, or you leave them open and that's unfair to the other questions AND a bit subjective. (What is a good discussion? Where to draw the line?)