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SHR Neuro Krebs Kardio Lipid

Damm, M; Nusshold, C; Cantillo, D; Rechberger, GN; Gruber, K; Sattler, W; Kappe, CO.
Can electromagnetic fields influence the structure and enzymatic digest of proteins? A critical evaluation of microwave-assisted proteomics protocols.
J Proteomics. 2012; 75(18):5533-5543 [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG


Autor/innen der Med Uni Graz:
Nusshold Christoph
Sattler Wolfgang

Dimensions Citations:

Plum Analytics:
Number of Figures: 5
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This 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 37-80 °C demonstrated that trypsin activity declines sharply at temperatures above 60 °C, regardless if microwave dielectric heating or conventional heating is employed. Tryptic digests of three proteins of different size (bovine serum albumin, cytochrome c and β-casein) were thus performed at 37 °C and 50 °C 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 3-4 orders of magnitude too low to induce conformational changes in proteins or enzymes.
Find related publications in this database (using NLM MeSH Indexing)
Caseins - chemistry
Computer Simulation -
Cytochromes c - chemistry
Electromagnetic Fields -
Electrophoresis, Polyacrylamide Gel -
Enzyme Stability -
Heating -
Hot Temperature -
Microwaves -
Models, Molecular -
Peptide Fragments - chemistry
Protein Conformation -
Proteomics - methods
Serum Albumin, Bovine - chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization -
Trypsin - metabolism

Find related publications in this database (Keywords)
Enzyme activity
Molecular mechanics calculations
Molecular modeling
Nonthermal microwave effects
Tryptic digest of proteins
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