{"id":9573,"date":"2012-08-06T09:03:39","date_gmt":"2012-08-06T07:03:39","guid":{"rendered":"https:\/\/web.computaex.es\/?page_id=9573"},"modified":"2025-08-27T09:35:35","modified_gmt":"2025-08-27T07:35:35","slug":"can-electromagnetic-fields-influence-the-structure-and-enzymatic-digest-of-proteins-a-critical-evaluation-of-microwave-assisted-proteomics-protocols","status":"publish","type":"page","link":"https:\/\/computaex.es\/en\/publicaciones\/can-electromagnetic-fields-influence-the-structure-and-enzymatic-digest-of-proteins-a-critical-evaluation-of-microwave-assisted-proteomics-protocols\/","title":{"rendered":"Can electromagnetic fields influence the structure and enzymatic digest of proteins? A critical evaluation of microwave-assisted proteomics protocols"},"content":{"rendered":"
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Markus Damm, Christoph Nusshold, David Cantillo, Gerald N. Rechberger, Karl Gruber, Wolfgang Sattler, C. Oliver Kappe.\u00a0Can electromagnetic fields influence the structure and enzymatic digest of proteins? A critical evaluation of microwave-assisted proteomics protocols<\/strong>. Journal of Proteomics. 2012. 1874-3919. doi: 10.1016\/j.jprot.2012.07.043.<\/p>\n

Abstract<\/strong>
\nThis study reevaluates the putative advantages of microwave-assisted tryptic digests compared to conventionally heated protocols performed at the same temperature. An initial investigation of enzyme stability in a temperature range of 37\u201380 \u00b0C demonstrated that trypsin activity declines sharply at temperatures above 60 \u00b0C, regardless if microwave dielectric heating or conventional heating is employed. Tryptic digests of three proteins of different size (bovine serum albumin, cytochrome\u00a0c<\/em>\u00a0and \u03b2-casein) were thus performed at 37\u00a0\u00b0C and 50\u00a0\u00b0C using both microwave and conventional heating applying accurate internal fiber-optic probe reaction temperature measurements. The impact of the heating method on protein degradation and peptide fragment generation was analyzed by SDS-PAGE and MALDI-TOF-MS. Time-dependent tryptic digestion of the three proteins and subsequent analysis of the corresponding cleavage products by MALDI-TOF provided virtually identical results for both microwave and conventional heating. In addition, the impact of electromagnetic field strength on the tertiary structure of trypsin and BSA was evaluated by molecular mechanics calculations. These simulations revealed that the applied field in a typical laboratory microwave reactor is 3\u20134 orders of magnitude too low to induce conformational changes in proteins or enzymes.<\/p>\n<\/div>\n<\/div>\n<\/div>\n

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