1. Phosphoryl Transfer Reaction Snapshots in Crystals: INSIGHTS INTO THE MECHANISM OF PROTEIN KINASE A CATALYTIC SUBUNIT.

    Journal of Biological Chemistry 290(25):15538 (2015) PMID 25925954 PMCID PMC4505467

    To study the catalytic mechanism of phosphorylation catalyzed by cAMP-dependent protein kinase (PKA) a structure of the enzyme-substrate complex representing the Michaelis complex is of specific interest as it can shed light on the structure of the transition state. However, all previous crystal...
  2. Determination of cellulose crystallinity from powder diffraction diagrams.

    Biopolymers 103(2):67 (2015) PMID 25269646

    One-dimensional (1D) (spherically averaged) powder diffraction diagrams are commonly used to determine the degree of cellulose crystallinity in biomass samples. Here, it is shown using molecular modeling how disorder in cellulose fibrils can lead to considerable uncertainty in conclusions drawn ...
  3. Determination of cellulose crystallinity from powder diffraction diagrams.

    Biopolymers 103(2):67 (2015) PMID 25269646

    One-dimensional (1D) (spherically averaged) powder diffraction diagrams are commonly used to determine the degree of cellulose crystallinity in biomass samples. Here, it is shown using molecular modeling how disorder in cellulose fibrils can lead to considerable uncertainty in conclusions drawn ...
  4. MARTINI coarse-grained model for crystalline cellulose microfibers.

    Journal of Physical Chemistry B 119(2):465 (2015) PMID 25417548

    Commercial-scale biofuel production requires a deep understanding of the structure and dynamics of its principal target: cellulose. However, an accurate description and modeling of this carbohydrate structure at the mesoscale remains elusive, particularly because of its overwhelming length scale...
  5. MARTINI coarse-grained model for crystalline cellulose microfibers.

    Journal of Physical Chemistry B 119(2):465 (2015) PMID 25417548

    Commercial-scale biofuel production requires a deep understanding of the structure and dynamics of its principal target: cellulose. However, an accurate description and modeling of this carbohydrate structure at the mesoscale remains elusive, particularly because of its overwhelming length scale...
  6. MARTINI Coarse-Grained Model for Crystalline Cellulose Microfibers.

    Journal of Physical Chemistry B 119(2):465 (2015) PMID 25417548

    Commercial-scale biofuel production requires a deep understanding of the structure and dynamics of its principal target: cellulose. However, an accurate description and modeling of this carbohydrate structure at the mesoscale remains elusive, particularly because of its overwhelming length scale...
  7. Why genetic modification of lignin leads to low-recalcitrance biomass.

    Physical Chemistry Chemical Physics 17(1):358 (2015) PMID 25384960

    Genetic modification of plants via down-regulation of cinnamyl alcohol dehydrogenase leads to incorporation of aldehyde groups in the lignin polymer. The resulting lignocellulosic biomass has increased bioethanol yield. However, a molecular-scale explanation of this finding is currently lacking....
  8. Why genetic modification of lignin leads to low-recalcitrance biomass.

    Physical Chemistry Chemical Physics 17(1):358 (2015) PMID 25384960

    Genetic modification of plants via down-regulation of cinnamyl alcohol dehydrogenase leads to incorporation of aldehyde groups in the lignin polymer. The resulting lignocellulosic biomass has increased bioethanol yield. However, a molecular-scale explanation of this finding is currently lacking....
  9. Toward resolving the catalytic mechanism of dihydrofolate reductase using neutron and ultrahigh-resolution X-ray crystallography.

    PNAS 111(51):18225 (2014) PMID 25453083 PMCID PMC4280638

    Dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate (DHF) to tetrahydrofolate (THF). An important step in the mechanism involves proton donation to the N5 atom of DHF. The inability to determine the protonation states of active site residues and substrate has ...
  10. Toward resolving the catalytic mechanism of dihydrofolate reductase using neutron and ultrahigh-resolution X-ray crystallography.

    PNAS 111(51):18225 (2014) PMID 25453083 PMCID PMC4280638

    Dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate (DHF) to tetrahydrofolate (THF). An important step in the mechanism involves proton donation to the N5 atom of DHF. The inability to determine the protonation states of active site residues and substrate has ...
  11. Toward resolving the catalytic mechanism of dihydrofolate reductase using neutron and ultrahigh-resolution X-ray crystallography.

    PNAS 111(51):18225 (2014) PMID 25453083 PMCID PMC4280638

    Dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate (DHF) to tetrahydrofolate (THF). An important step in the mechanism involves proton donation to the N5 atom of DHF. The inability to determine the protonation states of active site residues and substrate has ...
  12. Toward resolving the catalytic mechanism of dihydrofolate reductase using neutron and ultrahigh-resolution X-ray crystallography.

    PNAS 111(51):18225 (2014) PMID 25453083

    Dihydrofolate reductase (DHFR) catalyzes the NADPH-dependent reduction of dihydrofolate (DHF) to tetrahydrofolate (THF). An important step in the mechanism involves proton donation to the N5 atom of DHF. The inability to determine the protonation states of active site residues and substrate has ...
  13. Why genetic modification of lignin leads to low-recalcitrance biomass.

    Physical Chemistry Chemical Physics 17(1):358 (2014) PMID 25384960

    Genetic modification of plants via down-regulation of cinnamyl alcohol dehydrogenase leads to incorporation of aldehyde groups in the lignin polymer. The resulting lignocellulosic biomass has increased bioethanol yield. However, a molecular-scale explanation of this finding is currently lacking....
  14. Hydration control of the mechanical and dynamical properties of cellulose.

    Biomacromolecules 15(11):4152 (2014) PMID 25325376

    The mechanical and dynamical properties of cellulose, the most abundant biomolecule on earth, are essential for its function in plant cell walls and advanced biomaterials. Cellulose is almost always found in a hydrated state, and it is therefore important to understand how hydration influences i...
  15. Hydration control of the mechanical and dynamical properties of cellulose.

    Biomacromolecules 15(11):4152 (2014) PMID 25325376

    The mechanical and dynamical properties of cellulose, the most abundant biomolecule on earth, are essential for its function in plant cell walls and advanced biomaterials. Cellulose is almost always found in a hydrated state, and it is therefore important to understand how hydration influences i...
  16. Hydration control of the mechanical and dynamical properties of cellulose.

    Biomacromolecules 15(11):4152 (2014) PMID 25325376

    The mechanical and dynamical properties of cellulose, the most abundant biomolecule on earth, are essential for its function in plant cell walls and advanced biomaterials. Cellulose is almost always found in a hydrated state, and it is therefore important to understand how hydration influences i...
  17. L-Arabinose binding, isomerization, and epimerization by D-xylose isomerase: X-ray/neutron crystallographic and molecular simulation study.

    Structure 22(9):1287 (2014) PMID 25132082

    D-xylose isomerase (XI) is capable of sugar isomerization and slow conversion of some monosaccharides into their C2-epimers. We present X-ray and neutron crystallographic studies to locate H and D atoms during the respective isomerization and epimerization of L-arabinose to L-ribulose and L-ribo...
  18. Preliminary joint X-ray and neutron protein crystallographic studies of ecDHFR complexed with folate and NADP+.

    Acta crystallographica. Section F, Structural b... 70(Pt 6):814 (2014) PMID 24915100 PMCID PMC4051544

    A crystal of Escherichia coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP+ of 4×1.3×0.7 mm (3.6 mm3) in size was obtained by sequential application of microseeding and macroseeding. A neutron diffraction data set was collected to 2.0 Å resolution using the IMAGINE diffractome...
  19. Preliminary joint X-ray and neutron protein crystallographic studies of ecDHFR complexed with folate and NADP+.

    Acta crystallographica. Section F, Structural b... 70(Pt 6):814 (2014) PMID 24915100 PMCID PMC4051544

    A crystal of Escherichia coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP+ of 4×1.3×0.7 mm (3.6 mm3) in size was obtained by sequential application of microseeding and macroseeding. A neutron diffraction data set was collected to 2.0 Å resolution using the IMAGINE diffractome...
  20. Preliminary joint X-ray and neutron protein crystallographic studies of ecDHFR complexed with folate and NADP+.

    Acta crystallographica. Section F, Structural b... 70(Pt 6):814 (2014) PMID 24915100 PMCID PMC4051544

    A crystal of Escherichia coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP+ of 4×1.3×0.7 mm (3.6 mm3) in size was obtained by sequential application of microseeding and macroseeding. A neutron diffraction data set was collected to 2.0 Å resolution using the IMAGINE diffractome...