@article{AlrefaiMondalWrucketal.2019, author = {Alrefai, Anas and Mondal, Suvendu Sekhar and Wruck, Alexander and Kelling, Alexandra and Schilde, Uwe and Brandt, Philipp and Janiak, Christoph and Schoenfeld, Sophie and Weber, Birgit and Rybakowski, Lawrence and Herrman, Carmen and Brennenstuhl, Katlen and Eidner, Sascha and Kumke, Michael Uwe and Behrens, Karsten and G{\"u}nter, Christina and M{\"u}ller, Holger and Holdt, Hans-J{\"u}rgen}, title = {Hydrogen-bonded supramolecular metal-imidazolate frameworks: gas sorption, magnetic and UV/Vis spectroscopic properties}, series = {Journal of Inclusion Phenomena and Macrocyclic Chemistry}, volume = {94}, journal = {Journal of Inclusion Phenomena and Macrocyclic Chemistry}, number = {3-4}, publisher = {Springer}, address = {Dordrecht}, issn = {1388-3127}, doi = {10.1007/s10847-019-00926-6}, pages = {155 -- 165}, year = {2019}, abstract = {By varying reaction parameters for the syntheses of the hydrogen-bonded metal-imidazolate frameworks (HIF) HIF-1 and HIF-2 (featuring 14 Zn and 14 Co atoms, respectively) to increase their yields and crystallinity, we found that HIF-1 is generated in two different frameworks, named as HIF-1a and HIF-1b. HIF-1b is isostructural to HIF-2. We determined the gas sorption and magnetic properties of HIF-2. In comparison to HIF-1a (Brunauer-Emmett-Teller (BET) surface area of 471m(2) g(-1)), HIF-2 possesses overall very low gas sorption uptake capacities [BET(CO2) surface area=85m(2) g(-1)]. Variable temperature magnetic susceptibility measurement of HIF-2 showed antiferromagnetic exchange interactions between the cobalt(II) high-spin centres at lower temperature. Theoretical analysis by density functional theory confirmed this finding. The UV/Vis-reflection spectra of HIF-1 (mixture of HIF-1a and b), HIF-2 and HIF-3 (with 14 Cd atoms) were measured and showed a characteristic absorption band centered at 340nm, which was indicative for differences in the imidazolate framework.}, language = {en} } @inproceedings{KurbelNowakAzodietal.2015, author = {Kurbel, Karl and Nowak, Dawid and Azodi, Amir and Jaeger, David and Meinel, Christoph and Cheng, Feng and Sapegin, Andrey and Gawron, Marian and Morelli, Frank and Stahl, Lukas and Kerl, Stefan and Janz, Mariska and Hadaya, Abdulmasih and Ivanov, Ivaylo and Wiese, Lena and Neves, Mariana and Schapranow, Matthieu-Patrick and F{\"a}hnrich, Cindy and Feinbube, Frank and Eberhardt, Felix and Hagen, Wieland and Plauth, Max and Herscheid, Lena and Polze, Andreas and Barkowsky, Matthias and Dinger, Henriette and Faber, Lukas and Montenegro, Felix and Czach{\´o}rski, Tadeusz and Nycz, Monika and Nycz, Tomasz and Baader, Galina and Besner, Veronika and Hecht, Sonja and Schermann, Michael and Krcmar, Helmut and Wiradarma, Timur Pratama and Hentschel, Christian and Sack, Harald and Abramowicz, Witold and Sokolowska, Wioletta and Hossa, Tymoteusz and Opalka, Jakub and Fabisz, Karol and Kubaczyk, Mateusz and Cmil, Milena and Meng, Tianhui and Dadashnia, Sharam and Niesen, Tim and Fettke, Peter and Loos, Peter and Perscheid, Cindy and Schwarz, Christian and Schmidt, Christopher and Scholz, Matthias and Bock, Nikolai and Piller, Gunther and B{\"o}hm, Klaus and Norkus, Oliver and Clark, Brian and Friedrich, Bj{\"o}rn and Izadpanah, Babak and Merkel, Florian and Schweer, Ilias and Zimak, Alexander and Sauer, J{\"u}rgen and Fabian, Benjamin and Tilch, Georg and M{\"u}ller, David and Pl{\"o}ger, Sabrina and Friedrich, Christoph M. and Engels, Christoph and Amirkhanyan, Aragats and van der Walt, Est{\´e}e and Eloff, J. H. P. and Scheuermann, Bernd and Weinknecht, Elisa}, title = {HPI Future SOC Lab}, editor = {Meinel, Christoph and Polze, Andreas and Oswald, Gerhard and Strotmann, Rolf and Seibold, Ulrich and Schulzki, Bernhard}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-102516}, pages = {iii, 154}, year = {2015}, abstract = {Das Future SOC Lab am HPI ist eine Kooperation des Hasso-Plattner-Instituts mit verschiedenen Industriepartnern. Seine Aufgabe ist die Erm{\"o}glichung und F{\"o}rderung des Austausches zwischen Forschungsgemeinschaft und Industrie. Am Lab wird interessierten Wissenschaftlern eine Infrastruktur von neuester Hard- und Software kostenfrei f{\"u}r Forschungszwecke zur Verf{\"u}gung gestellt. Dazu z{\"a}hlen teilweise noch nicht am Markt verf{\"u}gbare Technologien, die im normalen Hochschulbereich in der Regel nicht zu finanzieren w{\"a}ren, bspw. Server mit bis zu 64 Cores und 2 TB Hauptspeicher. Diese Angebote richten sich insbesondere an Wissenschaftler in den Gebieten Informatik und Wirtschaftsinformatik. Einige der Schwerpunkte sind Cloud Computing, Parallelisierung und In-Memory Technologien. In diesem Technischen Bericht werden die Ergebnisse der Forschungsprojekte des Jahres 2015 vorgestellt. Ausgew{\"a}hlte Projekte stellten ihre Ergebnisse am 15. April 2015 und 4. November 2015 im Rahmen der Future SOC Lab Tag Veranstaltungen vor.}, language = {en} } @misc{VolkMarkertRiejoketal.2006, author = {Volk, Benno and Markert, Doreen and Riejok, Henriette and Dittberner, J{\"u}rgen and Wanka, Johanna and Wilkens, Martin and G{\"o}rtemaker, Manfred and Regierer, Babette and Steup, Martin and M{\"u}ller-R{\"o}ber, Bernd and Wernicke, Matthias and Altenberger, Uwe and St{\"o}lting, Erhard and Fer{\´y}, Carolin and Egenter, Peter and Lenz, Claudia and Jakubowski, Zuzanna and Kl{\"o}tzer, Sylvia and Krause, Michael and Dietsch, Ulrich}, title = {Portal = Vor der Pr{\"a}sidenten-Wahl: Erwartungen, W{\"u}nsche, Vorschl{\"a}ge}, number = {04-05/2006}, organization = {Universit{\"a}t Potsdam, Referat f{\"u}r Presse- und {\"O}ffentlichkeitsarbeit}, issn = {1618-6893}, doi = {10.25932/publishup-44000}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-440005}, pages = {50}, year = {2006}, abstract = {Aus dem Inhalt: - Vor der Pr{\"a}sidenten-Wahl: Erwartungen, W{\"u}nsche, Vorschl{\"a}ge - Der AStA in der Krise? - {\"U}ber Satire und Macht in der DDR - Vom F{\"u}nf-Sterne-Koch zum Mensaleiter}, language = {de} } @article{BroekerGohlkeMuelleretal.2013, author = {Br{\"o}ker, Nina Kristin and Gohlke, Ulrich and M{\"u}ller, J{\"u}rgen J. and Uetrecht, Charlotte and Heinemann, Udo and Seckler, Robert and Barbirz, Stefanie}, title = {Single amino acid exchange in bacteriophage HK620 tailspike protein results in thousand-fold increase of its oligosaccharide affinity}, series = {Glycobiology}, volume = {23}, journal = {Glycobiology}, number = {1}, publisher = {Oxford Univ. Press}, address = {Cary}, issn = {0959-6658}, doi = {10.1093/glycob/cws126}, pages = {59 -- 68}, year = {2013}, abstract = {Bacteriophage HK620 recognizes and cleaves the O-antigen polysaccharide of Escherichia coli serogroup O18A1 with its tailspike protein (TSP). HK620TSP binds hexasaccharide fragments with low affinity, but single amino acid exchanges generated a set of high-affinity mutants with submicromolar dissociation constants. Isothermal titration calorimetry showed that only small amounts of heat were released upon complex formation via a large number of direct and solvent-mediated hydrogen bonds between carbohydrate and protein. At room temperature, association was both enthalpy- and entropy-driven emphasizing major solvent rearrangements upon complex formation. Crystal structure analysis showed identical protein and sugar conformers in the TSP complexes regardless of their hexasaccharide affinity. Only in one case, a TSP mutant bound a different hexasaccharide conformer. The extended sugar binding site could be dissected in two regions: first, a hydrophobic pocket at the reducing end with minor affinity contributions. Access to this site could be blocked by a single aspartate to asparagine exchange without major loss in hexasaccharide affinity. Second, a region where the specific exchange of glutamate for glutamine created a site for an additional water molecule. Side-chain rearrangements upon sugar binding led to desolvation and additional hydrogen bonding which define this region of the binding site as the high-affinity scaffold.}, language = {en} } @article{SeulMuellerAndresetal.2014, author = {Seul, Anait and M{\"u}ller, J{\"u}rgen J. and Andres, Dorothee and Stettner, Eva and Heinemann, Udo and Seckler, Robert}, title = {Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker}, series = {Acta crystallographica : Section D, Biological crystallography}, volume = {70}, journal = {Acta crystallographica : Section D, Biological crystallography}, publisher = {Wiley-Blackwell}, address = {Hoboken}, issn = {1399-0047}, doi = {10.1107/S1399004714002685}, pages = {1336 -- 1345}, year = {2014}, abstract = {Attachment of phages to host cells, followed by phage DNA ejection, represents the first stage of viral infection of bacteria. Salmonella phage P22 has been extensively studied, serving as an experimental model for bacterial infection by phages. P22 engages bacteria by binding to the sugar moiety of lipopolysaccharides using the viral tailspike protein for attachment. While the structures of the N-terminal particle-binding domain and the major receptor-binding domain of the tailspike have been analyzed individually, the three-dimensional organization of the intact protein, including the highly conserved linker region between the two domains, remained unknown. A single amino-acid exchange in the linker sequence made it possible to crystallize the full-length protein. Two crystal structures of the linker region are presented: one attached to the N-terminal domain and the other present within the complete tailspike protein. Both retain their biological function, but the mutated full-length tailspike displays a retarded folding pathway. Fitting of the full-length tailspike into a published cryo-electron microscopy map of the P22 virion requires an elastic distortion of the crystal structure. The conservation of the linker suggests a role in signal transmission from the distal tip of the molecule to the phage head, eventually leading to DNA ejection.}, language = {en} } @article{CiemerBoersHirotaetal.2019, author = {Ciemer, Catrin and Boers, Niklas and Hirota, Marina and Kurths, J{\"u}rgen and M{\"u}ller-Hansen, Finn and Oliveira, Rafael S. and Winkelmann, Ricarda}, title = {Higher resilience to climatic disturbances in tropical vegetation exposed to more variable rainfall}, series = {Nature geoscience}, volume = {12}, journal = {Nature geoscience}, number = {3}, publisher = {Nature Publ. Group}, address = {New York}, issn = {1752-0894}, doi = {10.1038/s41561-019-0312-z}, pages = {174 -- 179}, year = {2019}, abstract = {With ongoing global warming, the amount and frequency of precipitation in the tropics is projected to change substantially. While it has been shown that tropical forests and savannahs are sustained within the same intermediate mean annual precipitation range, the mechanisms that lead to the resilience of these ecosystems are still not fully understood. In particular, the long-term impact of rainfall variability on resilience is as yet unclear. Here we present observational evidence that both tropical forest and savannah exposed to a higher rainfall variability-in particular on interannual scales-during their long-term past are overall more resilient against climatic disturbances. Based on precipitation and tree cover data in the Brazilian Amazon basin, we constructed potential landscapes that enable us to systematically measure the resilience of the different ecosystems. Additionally, we infer that shifts from forest to savannah due to decreasing precipitation in the future are more likely to occur in regions with a precursory lower rainfall variability. Long-term rainfall variability thus needs to be taken into account in resilience analyses and projections of vegetation response to climate change.}, language = {en} } @article{HoldtMuellerPotteretal.2006, author = {Holdt, Hans-J{\"u}rgen and M{\"u}ller, Holger and Potter, Matthias and Kelling, Alexandra and Schilde, Uwe and Starke, Ines and Heydenreich, Matthias and Kleinpeter, Erich}, title = {The first sandwich complex with an octa(thioether) coordination sphere : Bis(maleonitrile-tetrathia-12-crown- 4)silver(I)}, issn = {1434-1948}, doi = {10.1002/ejic.200501109}, year = {2006}, abstract = {The new tetrathiacrown ethers maleonitrile-tetrathia-12-crown-4 (mn12S(4)) and maleonitrile-tetrathia-13-crown- 4 (mn13S(4)) have been prepared and characterised by X-ray crystallographic analysis. These crown ethers form 2:1, 3:2 and 1: 1 complexes with AgY (Y = BF4, PF6). The crystal structures of [Ag(mn12S(4))(2)]BF4 (3a), [Ag(mn13S(4))(2)]BF4 (4a) and [Ag-2(mn13S(4))(3)](PF6)(2) (6b) have been determined. Compound 3a contains the centrosymmetric sandwich complex cation [Ag(mn12S(4))(2)](+) where each mn12S(4) ligand is coordinated to the Ag centre in an endo manner through all four S atoms. The 2:1 complex [Ag(mn12S(4))(2)](+) is the first sandwich complex with a tetrathiacrown ether and the first complex with an octa(thioether) coordination sphere. The crystal structure of compound 4a also reveals a 2:1 complex. This complex, [Ag(mnl3S(4))(2)](+), exhibits a half-sandwich structure. One mn13S(4) ligand coordinates to Ag+ by all four S donor atoms and the other 13S(4) crown by only one S atom. Compound 6b contains a dinuclear Ag complex. The Ag complexes 3a,b-8a,b were also studied by electrospray ionisation mass spectrometry. Collision-induced dissociation (CID) was used to compare the relative stability of 2:1 complexes [AgL2]+ and 1:1 complexes [AgL](+) (L = mn12S(4), mn13S(4)). The C-13 NMR chemical shifts of 2:1 and 1:1 Ag complexes and their corresponding free ligands were also estimated and compared. The free energy of the barrier of ring inversion (Delta G(double dagger)) for [Ag(mn12S(4))(2)](+) was determined to be 64 kJmol(-1).}, language = {en} } @article{StarkeFuerstenbergMuelleretal.2006, author = {Starke, Ines and F{\"u}rstenberg, Sylvia and M{\"u}ller, Holger and Holdt, Hans-J{\"u}rgen and Kleinpeter, Erich}, title = {Electrospray mass spectrometric studies of the complexational behavior of maleonitrile thiacrown ethers with various metals}, doi = {10.1002/Rcm.2384}, year = {2006}, abstract = {Electrospray ionization was employed to study the mass spectrometric behavior of the maleonitrile tetrathiacrown ethers mn12S(4) (1) and mn13S(4) (2) and maleonitrile pentathiacrown ether mn15S(5) (3) and of their complexes with various metal salts (MX2, M=Pd, Pt, Ni, Co, Fe; X=Cl, CrCl3, Ni(BF4)(2), TIPF6 or Cd(NO3)(2)) and Cu(SO3CF3)(2). Both singly charged, [MXL](+) and [MXL2]+, and doubly charged complexes, [MLn](2+) (n = 2-5), were observed. The formation of the different complexes consisting of the transition metal ion, the counterion and the various crown ethers and their subsequent dissociation was also studied by collision-induced dissociation measurements which were also used to evaluate the relative stabilities of the complexes. It was found that the collisional voltages for the dissociation of the complexes were generally greater in the [MXL](+) complexes than in the corresponding [MXL2]+ complexes. Copyright (c) 2006 John Wiley \& Sons, Ltd}, language = {en} } @article{BarbirzMuellerUetrechtetal.2008, author = {Barbirz, Stefanie and M{\"u}ller, J{\"u}rgen J. and Uetrecht, Charlotte and Clark, Alvin J. and Heinemann, Udo and Seckler, Robert}, title = {Crystal structure of Escherichia coli phage HK620 tailspike : podoviral tailspike endoglycosidase modules are evolutionarily related}, issn = {0950-382X}, year = {2008}, abstract = {Bacteriophage HK620 infects Escherichia coli H and is closely related to Shigella phage Sf6 and Salmonella phage P22. All three Podoviridae recognize and cleave their respective host cell receptor polysaccharide by homotrimeric tailspike proteins. The three proteins exhibit high sequence identity in the 110 residues of their N-terminal particle- binding domains, but no apparent sequence similarity in their major, receptor-binding parts. We have biochemically characterized the receptor-binding part of HK620 tailspike and determined its crystal structure to 1.38 {\AA} resolution. Its major domain is a right-handed parallel ;-helix, as in Sf6 and P22 tailspikes. HK620 tailspike has endo-N- acetylglucosaminidase activity and produces hexasaccharides of an O18A1-type O-antigen. As indicated by the structure of a hexasaccharide complex determined at 1.6 {\AA} resolution, the endoglycosidase-active sites are located intramolecularly, as in P22, and not between subunits, as in Sf6 tailspike. In contrast, the extreme C-terminal domain of HK620 tailspike forms a ;-sandwich, as in Sf6 and unlike P22 tailspike. Despite the different folds, structure-based sequence alignments of the C-termini reveal motifs conserved between the three proteins. We propose that the tailspike genes of P22, Sf6 and HK620 have a common precursor and are not mosaics of unrelated gene fragments.}, language = {en} } @article{MuellerBarbirzHeinleetal.2008, author = {M{\"u}ller, J{\"u}rgen J. and Barbirz, Stefanie and Heinle, Karolin and Freiberg, Alexander and Seckler, Robert and Heinemann, Udo}, title = {An intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of Shigella flexneri phage Sf6}, doi = {10.1016/j.str.2008.01.019}, year = {2008}, abstract = {Sf6 belongs to the Podoviridae family of temperate bacteriophages that infect gram-negative bacteria by insertion of their double-stranded DNA. They attach to their hosts specifically via their tailspike proteins. The 1.25 {\AA} crystal structure of Shigella phage Sf6 tailspike protein (Sf6 TSP) reveals a conserved architecture with a central, right-handed ; helix. In the trimer of Sf6 TSP, the parallel ; helices form a left-handed, coiled;; coil with a pitch of 340 {\AA}. The C-terminal domain consists of a ; sandwich reminiscent of viral capsid proteins. Further crystallographic and biochemical analyses show a Shigella cell wall O-antigen fragment to bind to an endorhamnosidase active site located between two ;-helix subunits each anchoring one catalytic carboxylate. The functionally and structurally related bacteriophage, P22 TSP, lacks sequence identity with Sf6 TSP and has its active sites on single subunits. Sf6 TSP may serve as an example for the evolution of different host specificities on a similar general architecture.}, language = {en} } @misc{MayerScharhagRosenbergerCarlsohnetal.2011, author = {Mayer, Frank and Scharhag-Rosenberger, Friederike and Carlsohn, Anja and Cassel, Michael and M{\"u}ller, Steffen and Scharhag, J{\"u}rgen}, title = {The intensity and effects of strength training in the elderly}, series = {Deutsches {\"A}rzteblatt international : a weekly online journal of clinical medicine and public health}, volume = {108}, journal = {Deutsches {\"A}rzteblatt international : a weekly online journal of clinical medicine and public health}, number = {21}, publisher = {Dt. {\"A}rzte-Verl.}, address = {Cologne}, issn = {1866-0452}, doi = {10.3238/arztebl.2011.0359}, pages = {359 -- U30}, year = {2011}, abstract = {Background: The elderly need strength training more and more as they grow older to stay mobile for their everyday activities. The goal of training is to reduce the loss of muscle mass and the resulting loss of motor function. The dose-response relationship of training intensity to training effect has not yet been fully elucidated. Methods: PubMed was selectively searched for articles that appeared in the past 5 years about the effects and dose-response relationship of strength training in the elderly. Results: Strength training in the elderly (> 60 years) increases muscle strength by increasing muscle mass, and by improving the recruitment of motor units, and increasing their firing rate. Muscle mass can be increased through training at an intensity corresponding to 60\% to 85\% of the individual maximum voluntary strength. Improving the rate of force development requires training at a higher intensity (above 85\%), in the elderly just as in younger persons. It is now recommended that healthy old people should train 3 or 4 times weekly for the best results; persons with poor performance at the outset can achieve improvement even with less frequent training. Side effects are rare. Conclusion: Progressive strength training in the elderly is efficient, even with higher intensities, to reduce sarcopenia, and to retain motor function.}, language = {en} } @article{MayerBonaventuraCasseletal.2012, author = {Mayer, Frank and Bonaventura, Klaus and Cassel, Michael and M{\"u}ller, Steffen and Weber, Josefine and Scharhag-Rosenberger, Friederike and Carlsohn, Anja and Baur, Heiner and Scharhag, J{\"u}rgen}, title = {Medical results of preparticipation examination in adolescent athletes}, series = {British journal of sports medicine : the journal of sport and exercise medicine}, volume = {46}, journal = {British journal of sports medicine : the journal of sport and exercise medicine}, number = {7}, publisher = {BMJ Publ. Group}, address = {London}, issn = {0306-3674}, doi = {10.1136/bjsports-2011-090966}, pages = {524 -- 530}, year = {2012}, abstract = {Background Preparticipation examinations (PPE) are frequently used to evaluate eligibility for competitive sports in adolescent athletes. Nevertheless, the effectiveness of these examinations is under debate since costs are high and its validity is discussed controversial. Purpose To analyse medical findings and consequences in adolescent athletes prior to admission to a sports school. Methods In 733 adolescent athletes (318 girls, 415 boys, age 12.3+/-0.4, 16 sports disciplines), history and clinical examination (musculoskeletal, cardiovascular, general medicine) was performed to evaluate eligibility. PPE was completed by determination of blood parameters, ECG at rest and during ergometry, echocardiography and x-rays and ultrasonography if indicated. Eligibility was either approved or rated with restriction. Recommendations for therapy and/or prevention were given to the athletes and their parents. Results Historical (h) and clinical (c) findings (eg, pain, verified pathologies) were more frequent regarding the musculoskeletal system (h: 120, 16.4\%; c: 247, 33.7\%) compared to cardiovascular (h: 9, 1.2\%; c: 23, 3.1\%) or general medicine findings (h: 116, 15.8\%; c: 71, 9.7\%). ECG at rest was moderately abnormal in 46 (6.3\%) and severely abnormal in 25 athletes (3.4\%). Exercise ECG was suspicious in 25 athletes (3.4\%). Relevant echocardiographic abnormalities were found in 17 athletes (2.3\%). In 52 of 358 cases (14.5\%), x-rays led to diagnosis (eg, Spondylolisthesis). Eligibility was temporarily restricted in 41 athletes (5.6\%). Three athletes (0.4\%) had to be excluded from competitive sports. Therapy (eg, physiotherapy, medication) and/or prevention (sensorimotor training, vaccination) recommendations were deduced due to musculoskeletal (t:n = 76,10.3\%; p:n = 71,9.8\%) and general medicine findings (t:n = 80, 10.9\%; p:n = 104, 14.1\%). Conclusion Eligibility for competitive sports is restricted in only 5.5\% of adolescent athletes at age 12. Eligibility refusals are rare. However, recommendations for therapy and prevention are frequent, mainly regarding the musculoskeletal system. In spite of time and cost consumption, adolescent preparticipation before entering a career in high-performance sports is supported.}, language = {en} }