Search: onr:"swepub:oai:DiVA.org:su-202027" > Charge Engineering ...
Fältnamn | Indikatorer | Metadata |
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000 | 05936naa a2200709 4500 | |
001 | oai:DiVA.org:su-202027 | |
003 | SwePub | |
008 | 220211s2021 | |||||||||||000 ||eng| | |
009 | oai:DiVA.org:uu-466905 | |
009 | oai:prod.swepub.kib.ki.se:234977906 | |
024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-2020272 URI |
024 | 7 | a https://doi.org/10.1021/jacsau.1c004582 DOI |
024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-4669052 URI |
024 | 7 | a http://kipublications.ki.se/Default.aspx?queryparsed=id:2349779062 URI |
040 | a (SwePub)sud (SwePub)uud (SwePub)ki | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a ref2 swepub-contenttype |
072 | 7 | a art2 swepub-publicationtype |
100 | 1 | a Abramsson, Mia L.u Karolinska Institutet4 aut |
245 | 1 0 | a Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry |
264 | c 2021-11-29 | |
264 | 1 | b American Chemical Society (ACS),c 2021 |
338 | a print2 rdacarrier | |
520 | a In solution, the charge of a protein is intricately linked to its stability, but electrospray ionization distorts this connection, potentially limiting the ability of native mass spectrometry to inform about protein structure and dynamics. How the behavior of intact proteins in the gas phase depends on the presence and distribution of ionizable surface residues has been difficult to answer because multiple chargeable sites are present in virtually all proteins. Turning to protein engineering, we show that ionizable side chains are completely dispensable for charging under native conditions, but if present, they are preferential protonation sites. The absence of ionizable side chains results in identical charge state distributions under native-like and denaturing conditions, while coexisting conformers can be distinguished using ion mobility separation. An excess of ionizable side chains, on the other hand, effectively modulates protein ion stability. In fact, moving a single ionizable group can dramatically alter the gas-phase conformation of a protein ion. We conclude that although the sum of the charges is governed solely by Coulombic terms, their locations affect the stability of the protein in the gas phase. | |
650 | 7 | a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng |
650 | 7 | a NATURVETENSKAPx Biologi0 (SwePub)1062 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciences0 (SwePub)1062 hsv//eng |
650 | 7 | a NATURVETENSKAPx Kemix Fysikalisk kemi0 (SwePub)104022 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Chemical Sciencesx Physical Chemistry0 (SwePub)104022 hsv//eng |
653 | a protein folding | |
653 | a gas-phase conformations | |
653 | a ion mobility mass spectrometry | |
700 | 1 | a Sahin, Caglau Karolinska Institutet4 aut |
700 | 1 | a Hopper, Jonathan T. S.u Univ Oxford, Dept Chem, Oxford OX1 3QZ, England.4 aut |
700 | 1 | a Branca, Rui M. M.u Karolinska Institutet4 aut |
700 | 1 | a Danielsson, Jensu Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, S-10691 Stockholm, Sweden.4 aut0 (Swepub:su)jedan |
700 | 1 | a Xu, Mingmingu Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, S-10691 Stockholm, Sweden.4 aut0 (Swepub:su)mixu4835 |
700 | 1 | a Chandler, Shane A.u Univ Oxford, Dept Chem, Oxford OX1 3QZ, England.4 aut |
700 | 1 | a Österlund, Nicklasu Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, S-10691 Stockholm, Sweden.4 aut0 (Swepub:su)nios7191 |
700 | 1 | a Ilag, Leopold L.u Stockholms universitet,Institutionen för material- och miljökemi (MMK),Stockholm Univ, Dept Mat & Environm Chem, S-10691 Stockholm, Sweden.4 aut0 (Swepub:su)lilag |
700 | 1 | a Leppert, Axelu Karolinska Inst, Dept Biosci & Nutr, S-14183 Huddinge, Sweden.4 aut |
700 | 1 | a Costeira-Paulo, Joanau Uppsala Univ, Dept Chem BMC, S-75123 Uppsala, Sweden.4 aut |
700 | 1 | a Lang, Lisau Stockholms universitet,Institutionen för biokemi och biofysik,Univ Oxford, Dept Chem, Oxford OX1 3QZ, England.4 aut0 (Swepub:su)lila2121 |
700 | 1 | a Teilum, Kaareu Univ Copenhagen, Linderstrom Lang Ctr Prot Sci, Dept Biol, DK-2200 Copenhagen, Denmark.4 aut |
700 | 1 | a Laganowsky, Arthuru Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA.4 aut |
700 | 1 | a Benesch, Justin L. P.4 aut |
700 | 1 | a Oliveberg, Mikaelu Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, S-10691 Stockholm, Sweden.4 aut0 (Swepub:su)moliv |
700 | 1 | a Robinson, Carol V.u Univ Oxford, Dept Chem, Oxford OX1 3QZ, England.4 aut |
700 | 1 | a Marklund, Erik,c Teknologie doktor,d 1979-u Uppsala universitet,Science for Life Laboratory, SciLifeLab,Biokemi4 aut0 (Swepub:uu)ermar499 |
700 | 1 | a Allison, Timothy M.u Univ Canterbury, Biomol Interact Ctr, Sch Phys & Chem Sci, Christchurch 8140, New Zealand.4 aut |
700 | 1 | a Winther, Jakob R.u Univ Copenhagen, Linderstrom Lang Ctr Prot Sci, Dept Biol, DK-2200 Copenhagen, Denmark.4 aut |
700 | 1 | a Landreh, Michaelu Karolinska Inst, Dept Microbiol Tumor & Cell Biol, S-17165 Stockholm, Sweden.4 aut |
710 | 2 | a Karolinska Institutetb Univ Oxford, Dept Chem, Oxford OX1 3QZ, England.4 org |
773 | 0 | t JACS Aud : American Chemical Society (ACS)g 1:12, s. 2385-2393q 1:12<2385-2393x 2691-3704 |
856 | 4 | u https://doi.org/10.1021/jacsau.1c00458y Fulltext |
856 | 4 | u https://pubs.acs.org/doi/pdf/10.1021/jacsau.1c00458 |
856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-202027 |
856 | 4 8 | u https://doi.org/10.1021/jacsau.1c00458 |
856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-466905 |
856 | 4 8 | u http://kipublications.ki.se/Default.aspx?queryparsed=id:234977906 |
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