ke ruan (11 risultati)

Soft cover. Condizione: New. BRAND NEW softcover. Book.

Condizione: New. pp. 156.

Taschenbuch. Condizione: Neu. Probing Protein Structural Dynamics from Residual Dipolar Couplings | De novo determination of protein structure and dynamics from multi-aligning residual dipolar couplings | Ke Ruan | Taschenbuch | 156 S. | Englisch | 2010 | LAP LAMBERT Academic Publishing | EAN 9783838303895 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.

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Paperback. Condizione: Good. No Jacket. Pages can have notes/highlighting. Spine may show signs of wear. ~ ThriftBooks: Read More, Spend Less.

Taschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Residual dipolar couplings (RDCs) provide explicit information of the molecular structure and dynamics in solution at atomic level. Full utilization of RDC datasets requires the acquisition under multiple aligning conditions, which remains experimentally challenging. We have illustrated in an application to ubiquitin that molecular alignment can be modified by varying the morphological characteristics of a composite medium, composed of ordered bacteriophage Pf1 particles embedded within stretched polyacrylamide gel matrix. The molecular alignment in this composite media could be adjusted by varying the angles between the directors of ordering for the Pf1 and strained gel, or by varying the concentrations of the components or magnesium. Since the acquisition of five independent RDC datasets still remains a difficulty, we develop a protocol that allows for the de novo determination of bond vector orientations from RDC measured in three independent alignment media assuming rigidity. The method proceeds by least squares optimization of both bond orientations and alignment tensors starting from an appropriately chosen initial 'guess'. 156 pp. Englisch.

Condizione: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Ruan KeKe Ruan received his B.S. and M.S. from Peking University. He earned his Ph.D. in Chemistry from Johns Hopkins University in 2008, focused on the characterization of protein structural dynamics by residual dipolar couplings. H.

Condizione: New. Print on Demand pp. 156 2:B&W 6 x 9 in or 229 x 152 mm Perfect Bound on Creme w/Gloss Lam.

Condizione: New. PRINT ON DEMAND pp. 156.

Taschenbuch. Condizione: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Residual dipolar couplings (RDCs) provide explicit information of the molecular structure and dynamics in solution at atomic level. Full utilization of RDC datasets requires the acquisition under multiple aligning conditions, which remains experimentally challenging. We have illustrated in an application to ubiquitin that molecular alignment can be modified by varying the morphological characteristics of a composite medium, composed of ordered bacteriophage Pf1 particles embedded within stretched polyacrylamide gel matrix. The molecular alignment in this composite media could be adjusted by varying the angles between the directors of ordering for the Pf1 and strained gel, or by varying the concentrations of the components or magnesium. Since the acquisition of five independent RDC datasets still remains a difficulty, we develop a protocol that allows for the de novo determination of bond vector orientations from RDC measured in three independent alignment media assuming rigidity. The method proceeds by least squares optimization of both bond orientations and alignment tensors starting from an appropriately chosen initial 'guess'.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 156 pp. Englisch.

Taschenbuch. Condizione: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Residual dipolar couplings (RDCs) provide explicit information of the molecular structure and dynamics in solution at atomic level. Full utilization of RDC datasets requires the acquisition under multiple aligning conditions, which remains experimentally challenging. We have illustrated in an application to ubiquitin that molecular alignment can be modified by varying the morphological characteristics of a composite medium, composed of ordered bacteriophage Pf1 particles embedded within stretched polyacrylamide gel matrix. The molecular alignment in this composite media could be adjusted by varying the angles between the directors of ordering for the Pf1 and strained gel, or by varying the concentrations of the components or magnesium. Since the acquisition of five independent RDC datasets still remains a difficulty, we develop a protocol that allows for the de novo determination of bond vector orientations from RDC measured in three independent alignment media assuming rigidity. The method proceeds by least squares optimization of both bond orientations and alignment tensors starting from an appropriately chosen initial 'guess'.