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  • 1.
    Blom, Hans
    et al.
    KTH, Skolan för teknikvetenskap (SCI), Tillämpad fysik, Cellens fysik. KTH, Centra, Science for Life Laboratory, SciLifeLab.
    Widengren, Jerker
    KTH, Skolan för teknikvetenskap (SCI), Tillämpad fysik, Experimentell biomolekylär fysik.
    STED microscopy: towards broadened use and scope of applications2014Ingår i: Current opinion in chemical biology, ISSN 1367-5931, E-ISSN 1879-0402, Vol. 20, nr 1, s. 127-133Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    High resolution Stimulated Emission Depletion (STED) microscopy has been demonstrated for fundamental studies in cells, living tissue and organisms. Today, a major trend in the STED technique development is to make the instruments simpler and more user-friendly, without compromising performance. This has become possible by new low-cost, turn-key laser technology and by implementing specifically designed phase plates and polarization elements, extending and simplifying the shaping of the laser beam profiles. These simpler and cheaper realizations of STED are now becoming more broadly available. In parallel with the continuous development of sample preparation and fluorophore reporter molecules ultimately setting the limit of the image quality, contrast and resolution, we can thus expect a significant increase in the use of STED, in science as well as for clinical and drug development purposes.

  • 2. Cheon, Seungwoo
    et al.
    Kim, Hye Mi
    Gustavsson, Martin
    KTH, Skolan för bioteknologi (BIO), Bioprocessteknik (stängd 20130101).
    Lee, Sang Yup
    Recent trends in metabolic engineering of microorganisms for the production of advanced biofuels2016Ingår i: Current opinion in chemical biology, ISSN 1367-5931, E-ISSN 1879-0402, Vol. 35, s. 10-21Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    As climate change has become one of the major global risks, our heavy dependence on petroleum-derived fuels has received much public attention. To solve such problems, production of sustainable fuels has been intensively studied over the past years. Thanks to recent advances in synthetic biology and metabolic engineering technologies, bio-based platforms for advanced biofuels production have been developed using various microorganisms. The strategies for production of advanced biofuels have converged upon four major metabolic routes: the 2-ketoacid pathway, the fatty acid synthesis (FAS) pathway, the isoprenoid pathway, and the reverse β-oxidation pathway. Additionally, the polyketide synthesis pathway has recently been attracting interest as a promising alternative biofuel production route. In this article, recent trends in advanced biofuels production are reviewed by categorizing them into three types of advanced biofuels: alcohols, biodiesel and jet fuel, and gasoline. Focus is given on the strategies of employing synthetic biology and metabolic engineering for the development of microbial strains producing advanced fuels. Finally, the prospects for future advances needed to achieve much more efficient bio-based production of advanced biofuels are discussed, focusing on designing advanced biofuel production pathways coupled with screening, modifying, and creating novel enzymes.

  • 3. Fink, Michael J.
    et al.
    Syrén, Per-Olof
    KTH, Skolan för bioteknologi (BIO), Proteomik och nanobioteknologi. KTH, Centra, Science for Life Laboratory, SciLifeLab. KTH, Skolan för kemivetenskap (CHE), Kemi, Tillämpad fysikalisk kemi.
    Redesign of water networks for efficient biocatalysis2017Ingår i: Current opinion in chemical biology, ISSN 1367-5931, E-ISSN 1879-0402, Vol. 37, s. 107-114Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Herein we highlight recent findings on the importance of water networks in proteins, and their redesign and reconfiguration as a new engineering strategy to generate enzymes with modulated binding affinity and improved catalytic versatility. Traditionally, enzyme engineering and drug design have focused on tailoring direct and favorable interactions between protein surfaces and ligands/transition states to achieve stronger binding, or an accelerated manufacturing of medicines, biofuels, fine chemicals and materials. In contrast, the opportunity to relocate water molecules in solvated binding pockets by protein design to improve overall energetics remains essentially unexplored, and fundamental understanding of the elusive processes involved is poor. Rewiring water networks in protein interiors impacts binding affinity, catalysis and the thermodynamic signature of biochemical processes through dynamic mechanisms, and thus has great potential to enhance binding specificity, accelerate catalysis and provide new reaction mechanisms and chemistry, that were not yet explored in nature.

  • 4. Hammer, Stephan C.
    et al.
    Syren, Per-Olof
    Universitaet Stuttgart, Germany.
    Seitz, Miriam
    Nestl, Bettina M.
    Hauer, Bernhard
    Squalene hopene cyclases: highly promiscuous and evolvable catalysts for stereoselective CC and CX bond formation2013Ingår i: Current opinion in chemical biology, ISSN 1367-5931, E-ISSN 1879-0402, Vol. 17, nr 2, s. 293-300Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    A review. We review here how the inherent promiscuous nature, as well as the evolvability of terpene cyclase enzymes enables new applications in chem. We mainly focus on squalene hopene cyclases, class II triterpene synthases that use a proton-initiated cationic polycyclization cascade to form carbopolycyclic products. We highlight recent findings to demonstrate that these enzymes are capable of activating different functionalities other than the traditional terminal isoprene CC-group as well as being compatible with a wide range of nucleophiles beyond the 'ene-functionality'. Thus, squalene hopene cyclases demonstrate a great potential to be used as a toolbox for general Bronsted acid catalysis.

  • 5. Kohls, Hannes
    et al.
    Steffen-Munsberg, Fabian
    KTH, Skolan för bioteknologi (BIO), Industriell bioteknologi.
    Hoehne, Matthias
    Recent achievements in developing the biocatalytic toolbox for chiral amine synthesis2014Ingår i: Current opinion in chemical biology, ISSN 1367-5931, E-ISSN 1879-0402, Vol. 19, s. 180-192Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Novel enzyme activities and chemoenzymatic reaction concepts have considerably expanded the biocatalytic toolbox for chiral amine synthesis. Creating new activities or extending the scope of existing enzymes by protein engineering is a common trend in biocatalysis and in chiral amine synthesis specifically. For instance, an amine dehydrogenase that allows for the direct asymmetric amination of ketones with ammonia was created by mutagenesis of an L-amino acid dehydrogenase. Another trend in chiral amine chemistry is the development of strategies allowing for the synthesis of secondary amines. For example the smart choice of substrates for amine transaminases provided access to secondary amines by chemoenzymatic reactions. Furthermore novel biocatalysts for the synthesis of secondary amines such as imine reductases and Pictet-Spenglerases have been identified and applied. Recent examples showed that the biocatalytic amine synthesis is emerging from simple model reactions towards industrial scale preparation of pharmaceutical relevant substances, for instance, as shown in the synthesis of a Janus kinase 2 inhibitor using an amine transaminase. A comparison of important process parameters such as turnover number and space-time yield demonstrates that biocatalytic strategies for asymmetric reductive amination are maturing and can already compete with established chemical methods.

  • 6.
    Mahecic, Dora
    et al.
    Ecole Polytech Fed Lausanne, Lab Expt Biophys, Inst Phys, CH-1015 Lausanne, Switzerland..
    Testa, Ilaria
    KTH, Skolan för teknikvetenskap (SCI), Tillämpad fysik. KTH, Centra, Science for Life Laboratory, SciLifeLab.
    Griffie, Juliette
    Ecole Polytech Fed Lausanne, Lab Expt Biophys, Inst Phys, CH-1015 Lausanne, Switzerland..
    Manley, Suliana
    Ecole Polytech Fed Lausanne, Lab Expt Biophys, Inst Phys, CH-1015 Lausanne, Switzerland..
    Strategies for increasing the throughput of super-resolution microscopies2019Ingår i: Current opinion in chemical biology, ISSN 1367-5931, E-ISSN 1879-0402, Vol. 51, s. 84-91Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Fluorescence microscopy methods have been developed to circumvent the diffraction limit by exploiting nonlinearities in the interactions between light and fluorophores. Initially, these methods were up to orders of magnitude slower than standard microscopies. In recent years, a wide array of technological advances have increased the throughput of super-resolution microscopies, through parallelization, smart scanning or data processing, and sample expansion. Here, we review re cent innovations for increased throughput, some applications that have benefitted from them, and how they could be improved in the future.

  • 7. Noodleman, L.
    et al.
    Lovell, T.
    Liu, T. Q.
    Himo, Fahmi
    KTH, Tidigare Institutioner                               , Bioteknologi.
    Torres, R. A.
    Insights into properties and energetics of iron-sulfur proteins from simple clusters to nitrogenase2002Ingår i: Current opinion in chemical biology, ISSN 1367-5931, E-ISSN 1879-0402, Vol. 6, nr 2, s. 259-273Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Some of the principal physical features of iron-sulfur clusters in proteins are analyzed, including metal-ligand covalency, spin polarization, spin coupling, valence delocalization, valence interchange and small reorganization energies, with emphasis on recent spectroscopic and theoretical work. The current state of structural, spectroscopic, and computational knowledge for the iron-sulfur clusters in the nitrogenase iron and iron-molybdenum proteins is examined by comparison and contrast to 'simpler' iron-sulfur clusters. The differing interactions of the nitrogenase iron and iron-molybdenum clusters compared with those of other iron-sulfur clusters with the protein and solvent environment are also explored.

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