Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

Przeglądasz jako GOŚĆ

Wyszukujesz frazę ""Bacterial Proteins chemistry"" wg kryterium: Temat


Tytuł :
Mapping the ultrafast vibrational dynamics of all- trans and 13- cis retinal isomerization in Anabaena Sensory Rhodopsin
Autorzy :
Roy, Partha Pratim
Kato, Youshitoka
Abe-Yoshizumi, Rei
Pieri, Elisa
Ferré, Nicolas
Kandori, Hideki
Buckup, Tiago
Pokaż więcej
Temat :
Anabaena/chemistry
Bacterial Proteins/chemistry
Retinaldehyde/chemistry
Sensory Rhodopsins/chemistry
Stereoisomerism
Vibration
[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry
Źródło :
Physical Chemistry Chemical Physics
Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2018, 20 (48), pp.30159-30173. ⟨10.1039/c8cp05469j⟩
Tytuł :
Mapping the ultrafast vibrational dynamics of all- trans and 13- cis retinal isomerization in Anabaena Sensory Rhodopsin
Autorzy :
Roy, Partha Pratim
Kato, Youshitoka
Abe-Yoshizumi, Rei
Pieri, Elisa
Ferré, Nicolas
Kandori, Hideki
Buckup, Tiago
Pokaż więcej
Temat :
[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry
[ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistry
Anabaena/chemistry
Stereoisomerism
Retinaldehyde/chemistry
Vibration
Sensory Rhodopsins/chemistry
Bacterial Proteins/chemistry
Źródło :
Physical Chemistry Chemical Physics
Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2018, 20 (48), pp.30159-30173. ⟨10.1039/c8cp05469j⟩
Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2018, 20 (48), pp.30159-30173. 〈10.1039/c8cp05469j〉
Tytuł :
Membrane association and remodeling by intraflagellar transport protein IFT172
Autorzy :
Ganzinger, Kristina A.
Kelley, Charlotte
Heymann, Michael
Schwille, Petra
Mizuno, Naoko
Wang, Qianmin
Taschner, Michael
Villasenor, Alethia
Lorentzen, Esben
Pokaż więcej
Temat :
Bacterial Proteins/chemistry
Bacterial Proteins/metabolism
Bacterial Proteins/ultrastructure
Cell Membrane/metabolism
Cell Membrane/ultrastructure
Chlamydomonas
Flagella/metabolism
Lipids/chemistry
Liposomes
Membrane Proteins/chemistry
Membrane Proteins/metabolism
Protein Binding
Protein Conformation
Recombinant Proteins/metabolism
Science
sense organs
Article
Źródło :
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Wang, Q, Taschner, M, Ganzinger, K A, Kelley, C, Villasenor, A, Heymann, M, Schwille, P, Lorentzen, E & Mizuno, N 2018, ' Membrane association and remodeling by intraflagellar transport protein IFT172 ', Nature Communications, vol. 9, no. 1, 4684 . https://doi.org/10.1038/s41467-018-07037-9
Nature communications, vol. 9, no. 1, pp. 4684
Opis pliku :
application/pdf
Tytuł :
Mapping the contact sites of the escherichia coli division-initiating proteins FtsZ and ZapA by BAMG cross-linking and site-directed mutagenesis
Autorzy :
Roseboom, Winfried
Nazir, Madhvi G.
Meiresonne, Nils Y.
Mohammadi, Tamimount
Verheul, Jolanda
Buncherd, Hansuk
Bonvin, Alexandre M. J. J.
Koning, Leo J. de
Koster, Chris G. de
Jong, Luitzen de
Blaauwen, Tanneke den
Pokaż więcej
Temat :
Molecular Biology
1,4-bis(succimidyl)-3-azidomethylglutarate (BAMG)
Lysine/chemistry
Z associated protein A (ZapA)
Software
bacteria
biological phenomena, cell phenomena, and immunity
QD1-999
Catalysis
Escherichia coli Proteins/chemistry
Filamenting temperature sensitive Z (FtsZ)
Amino Acid Sequence
Escherichia coli/genetics
Molecular Docking Simulation
Spectroscopy
Organic Chemistry
Cross-Linking Reagents/chemistry
Computer Science Applications
Binding Sites/genetics
Chemistry
Fourier-transform ion cyclotron resonance mass spectrometry(FTICR)
Inorganic Chemistry
Protein Multimerization
Cell division
Cytoskeletal Proteins/chemistry
Mass Spectrometry/methods
Protein Binding
Protein Domains
Quadrupole time of flight mass spectrometer (QTOF)
Carrier Proteins/chemistry
Article
QH301-705.5
Physical and Theoretical Chemistry
macromolecular substances
Cell Division/genetics
physiological processes
Mutagenesis, Site-Directed/methods
Biology (General)
Bacterial Proteins/chemistry
Źródło :
International Journal of Molecular Sciences, Vol 19, Iss 10, p 2928 (2018)
International Journal of Molecular Sciences, 19(10)
International Journal of Molecular Sciences
International Journal of Molecular Sciences, 19(10). Multidisciplinary Digital Publishing Institute (MDPI)
Opis pliku :
application/pdf; text/plain
Tytuł :
Structural changes of TasA in biofilm formation of Bacillus subtilis
Autorzy :
van Rossum, Barth-Jan
Heinemann, Udo
Turgay, Kürşad
Diehl, Anne
Roske, Yvette
Ball, Linda
Chowdhury, Anup
Hiller, Matthias
Molière, Noel
Kramer, Regina
Stöppler, Daniel
Worth, Catherine L.
Schlegel, Brigitte
Leidert, Martina
Cremer, Nils
Erdmann, Natalja
Lopez, Daniel
Stephanowitz, Heike
Krause, Eberhard
Schmieder, Peter
Akbey, Ümit
Oschkinat, Hartmut
Pokaż więcej
Temat :
Metalloendopeptidases/chemistry
CEREUS
Magnetic Resonance Spectroscopy
MATRIX
TasA
Microscopy, Electron
Cancer Research
MASTER REGULATOR
Models, Molecular
NMR
IDENTIFICATION
Physical Sciences
SIGNAL PEPTIDASE
Hydrogen-Ion Concentration
biofilm
PROTEIN
POLYPROLINE-II HELIX
MECHANISMS
Calorimetry
SURFACE
Bacillus subtilis/chemistry
Ultracentrifugation
Biofilms/growth & development
Biophysics and Computational Biology
Bacillus subtilis
Microbiology
Protein Conformation
Molecular Weight
AMYLOID FIBERS
structure
Biological Sciences
Crystallography, X-Ray
Structural Homology, Protein
ddc:000
ddc:500
Bacterial Proteins/chemistry
Źródło :
Proceedings of the National Academy of Sciences of the United States of America 115 (2018), Nr. 13
Diehl, A, Roske, Y, Ball, L, Chowdhury, A, Hiller, M, Moliere, N, Kramer, R, Stoeppler, D, Worth, C L, Schlegel, B, Leidert, M, Cremer, N, Erdmann, N, Lopez, D, Stephanowitz, H, Krause, E, van Rossum, B-J, Schmieder, P, Heinemann, U, Turgay, K, Akbey, U & Oschkinat, H 2018, ' Structural changes of TasA in biofilm formation of Bacillus subtilis ', Proceedings of the National Academy of Sciences of the United States of America, vol. 115, no. 13, pp. 3237-3242 . https://doi.org/10.1073/pnas.1718102115
Proceedings of the National Academy of Sciences of the United States of America
Opis pliku :
application/pdf
Tytuł :
Interplay between the catabolite repression control protein Crc, Hfq and RNA in Hfq-dependent translational regulation in Pseudomonas aeruginosa
Autorzy :
Wolfinger, Michael T
Luisi, Bonaventura
Sonnleitner, Elisabeth
Wulf, Alexander
Campagne, Sébastien
Pei, Xue-Yuan
Forlani, Giada
Prindl, Konstantin
Abdou, Laetitia
Resch, Armin
Allain, Frederic H-T
Urlaub, Henning
Bläsi, Udo
Pokaż więcej
Temat :
Repressor Proteins
Bacterial Proteins/chemistry
Bacterial Proteins/genetics
Bacterial Proteins/metabolism
Binding Sites
Bordetella pertussis/genetics
Bordetella pertussis/metabolism
Carbohydrate Metabolism/genetics
Catabolite Repression
Escherichia coli/genetics
Escherichia coli/metabolism
Gene Expression Regulation, Bacterial
Host Factor 1 Protein/chemistry
Host Factor 1 Protein/genetics
Host Factor 1 Protein/metabolism
Kinetics
Models, Molecular
Nucleotide Motifs
Protein Binding
Protein Biosynthesis
Protein Interaction Domains and Motifs
Protein Structure, Secondary
Pseudomonas aeruginosa/genetics
Pseudomonas aeruginosa/metabolism
RNA, Bacterial/chemistry
RNA, Bacterial/genetics
RNA, Bacterial/metabolism
Regulon
Repressor Proteins/chemistry
Repressor Proteins/genetics
Repressor Proteins/metabolism
Transcriptome
Pseudomonas aeruginosa
Bacterial Proteins
Escherichia coli
Carbohydrate Metabolism
Bordetella pertussis
digestive system diseases
Host Factor 1 Protein
RNA Prot Comp
neoplasms
RNA, Bacterial
Źródło :
Nucleic acids research, 46 (3)
Nucleic acids research, vol. 46, no. 3, pp. 1470-1485
Opis pliku :
application/pdf; Print; application/application/pdf

Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies