#trypsin — Public Fediverse posts
Live and recent posts from across the Fediverse tagged #trypsin, aggregated by home.social.
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quantum computers can be networked now, more usable qubits will be able to be connected
more 'breakthroughs' will end up happening, things go slow at the start
#ibm #cleveland clinic #folding #enzymes #trypsin #catalysts #sims #merck index #buffer systems #chirality #nextplatform.com
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quantum computers can be networked now, more usable qubits will be able to be connected
more 'breakthroughs' will end up happening, things go slow at the start
#ibm #cleveland clinic #folding #enzymes #trypsin #catalysts #sims #merck index #buffer systems #chirality #nextplatform.com
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quantum computers can be networked now, more usable qubits will be able to be connected
more 'breakthroughs' will end up happening, things go slow at the start
#ibm #cleveland clinic #folding #enzymes #trypsin #catalysts #sims #merck index #buffer systems #chirality #nextplatform.com
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quantum computers can be networked now, more usable qubits will be able to be connected
more 'breakthroughs' will end up happening, things go slow at the start
#ibm #cleveland clinic #folding #enzymes #trypsin #catalysts #sims #merck index #buffer systems #chirality #nextplatform.com
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The structure of an M26 IgA1 protease trypsin-like domain suggests that this domain may exist in a pro-enzyme-like state in the full-length protein @uWaterloo @ActaCrystF @IUCr #IgAProteases #SerineProteases #Trypsin https://doi.org/10.1107/S2053230X25001219
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The structure of an M26 IgA1 protease trypsin-like domain suggests that this domain may exist in a pro-enzyme-like state in the full-length protein @uWaterloo @ActaCrystF @IUCr #IgAProteases #SerineProteases #Trypsin https://doi.org/10.1107/S2053230X25001219
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The structure of an M26 IgA1 protease trypsin-like domain suggests that this domain may exist in a pro-enzyme-like state in the full-length protein @uWaterloo @ActaCrystF @IUCr #IgAProteases #SerineProteases #Trypsin https://doi.org/10.1107/S2053230X25001219
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I use the #surfactant #SDC extensively for #proteomics sample prep. It is compatible with #Trypsin and easily removed. Very occasionally the solution will gel - and I can reverse this fortunately. Today I discovered why this happens:
https://doi.org/10.1021/jp409626s
"The results demonstrate that the gels are formed by intertwined fibrils, which are induced by enormous cycles of NaDC molecules driven by comprehensive noncovalent interactions, especially the hydrogen bonds." -
I use the #surfactant #SDC extensively for #proteomics sample prep. It is compatible with #Trypsin and easily removed. Very occasionally the solution will gel - and I can reverse this fortunately. Today I discovered why this happens:
https://doi.org/10.1021/jp409626s
"The results demonstrate that the gels are formed by intertwined fibrils, which are induced by enormous cycles of NaDC molecules driven by comprehensive noncovalent interactions, especially the hydrogen bonds." -
I use the #surfactant #SDC extensively for #proteomics sample prep. It is compatible with #Trypsin and easily removed. Very occasionally the solution will gel - and I can reverse this fortunately. Today I discovered why this happens:
https://doi.org/10.1021/jp409626s
"The results demonstrate that the gels are formed by intertwined fibrils, which are induced by enormous cycles of NaDC molecules driven by comprehensive noncovalent interactions, especially the hydrogen bonds." -
I use the #surfactant #SDC extensively for #proteomics sample prep. It is compatible with #Trypsin and easily removed. Very occasionally the solution will gel - and I can reverse this fortunately. Today I discovered why this happens:
https://doi.org/10.1021/jp409626s
"The results demonstrate that the gels are formed by intertwined fibrils, which are induced by enormous cycles of NaDC molecules driven by comprehensive noncovalent interactions, especially the hydrogen bonds."