P
Peter Brzezinski
Researcher at Stockholm University
Publications - 206
Citations - 11720
Peter Brzezinski is an academic researcher from Stockholm University. The author has contributed to research in topics: Cytochrome c oxidase & Electron transfer. The author has an hindex of 49, co-authored 198 publications receiving 11056 citations. Previous affiliations of Peter Brzezinski include University of Mississippi Medical Center & University of Illinois at Urbana–Champaign.
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Quartz crystal microbalance setup for frequency and Q‐factor measurements in gaseous and liquid environments
TL;DR: In this paper, an experimental setup has been constructed for simultaneous measurements of the frequency, the absolute Q factor, and the amplitude of oscillation of a quartz crystal microbalance (QCM).
Quartz crystal microbalance setup for frequency and G!?-factor rneasurements in gaseous and liquid environments
TL;DR: In this paper, an experimental setup has been constructed for simultaneous measurements of the frequency, the absolute Q factor, and the amplitude of oscillation of a quartz crystal microbalance (QCM).
Journal ArticleDOI
Simultaneous frequency and dissipation factor QCM measurements of biomolecular adsorption and cell adhesion
Michael Rodahl,Fredrik Höök,Claes Fredriksson,Craig A. Keller,Anatol Krozer,Peter Brzezinski,M. V. Voinova,Bengt Herbert Kasemo +7 more
TL;DR: It is shown theoretically that viscoelastic layers with thicknesses comparable to the biofilms studied in this work can induce energy dissipation of the same magnitude as the measured ones.
Journal ArticleDOI
Energy Dissipation Kinetics for Protein and Antibody−Antigen Adsorption under Shear Oscillation on a Quartz Crystal Microbalance
TL;DR: In this article, a new quartz crystal microbalance instrument, allowing simultaneous frequency (f) and dissipation factor (D) measurements, has been used to study protein adsorption kinetics by measuring time-resolved data of both the D-factor, measuring energy dissipation due to the added overlayer, and the f-shift, measuring the effective mass load on the sensor.
Journal ArticleDOI
The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides.
Margareta Svensson-Ek,Jeff Abramson,Gisela Larsson,Gisela Larsson,Susanna Törnroth,Peter Brzezinski,So Iwata,So Iwata +7 more
TL;DR: The structure of cytochrome c oxidase from Rhodobacter sphaeroides has been solved at 2.3/2.8A (anisotropic resolution) and atomic details of a bacterial terminal oxidase including water molecule positions and a potential oxygen pathway are revealed.