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  • 1
    Electronic Resource
    Electronic Resource
    Scanning tunneling microscopy of the GaN(000 〈 ![IGNORE[$\bar{1}$]] ) surface (1998)
    Springer
    Applied physics 66 (1998), S. S947 
    Details
    ISSN: 1432-0630
    Keywords: PACS: 68.35.Bs; 68.55.Jk; 61.16.Ch
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: ) surface. Four dominant reconstructions have been observed: 1×1, 3×3, 6×6, and c(6×12). The 1×1 structure is formed by annealing the as-grown GaN surface to desorb excess Ga atoms. The higher-order reconstructions are formed by depositing sub-monolayer quantities of Ga atoms onto this 1×1surface. STM images showing the details of the reconstructions are presented and results of quantitative measurements of the number of Ga atoms required to form the various reconstructions are reported. Structural models are compared with the STM data. Reversible order/disorder phase transitions and adatom motion on the GaN surface are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003390051272
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  • 2
    Electronic Resource
    Electronic Resource
    Brownian dynamics simulation of protein association (1988)
    Springer
    Journal of computer aided molecular design 1 (1988), S. 291-311 
    Details
    ISSN: 1573-4951
    Keywords: Protein electrostatics ; Electron transfer ; Heme proteins ; Brownian dynamics ; Diffusion-controlled reactions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The Brownian Dynamics (BD) method is applied to study the diffusive dynamics and interaction of two proteins, cytochrome c (CYTC) and cytochrome c peroxidase (CYP). We examine the role of protein electrostatic charge distribution in the facilitation of protein-protein docking prior to the electron transfer step, assessing the influence of individual charged amino acid residues. Accurate interaction potentials are computed by iterating the linearized Poisson-Boltzmann (PB) equation around the larger protein CYP. The low dielectric constant inside proteins, electrolyte screening effects and irregular protein surface topography are taken into account. We observe a large ensemble of electrostatically stable encounter complexes seemingly with acceptable geometric requirements for electron transfer rather than a single dominant complex. Stabilities of the large variety of docking complexes are rationalized in terms of generalized charged residue complementarities. However, it is found that the electrostatic interactions giving rise to complex stabilities are somewhat nonspecific in nature. A large series of additional simulations are performed in which individual charged residues on CYTC have been chemically modified. Resulting perturbations of the association rate are significant and qualitatively similar to results observed in comparable kinetics experiments. We therefore demonstrate the potential of the Brownian dynamics method to estimate the effects of site-directed mutagenesis on protein-protein and protein-ligand diffusional association rates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01677278
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    Paper (German National Licenses)
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