Conformation Tensor
Mostrando 1-5 de 5 artigos, teses e dissertações.
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1. ESTABILIDADE DO ESCOAMENTO VISCOELÁSTICO EM PROCESSO DE REVESTIMENTO POR ROTAÇÃO DIRETA / STABILITY OF VISCOELASTIC FORWARD ROLL COATING FLOWS
O processo de revestimento por rotação é caracterizado pelo uso de cilindros girantes para controlar a espessura e aplicar uma fina camada de líquido em um substrato em movimento. A não ser a baixas velocidades dos cilindros, o escoamento bi-dimensional na região de formação dos filmes sobre cada cilindro é instável e o padrão observado experiment
Publicado em: 2003
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2. A spectroscopic method for observing the domain movement of the Rieske iron–sulfur protein
The g-tensor orientation of the chemically reduced Rieske cluster in cytochrome bc1 complex from Rhodovulum sulfidophilum with respect to the membrane was determined in the presence and absence of inhibitors and in the presence of oxidized and reduced quinone in the quinol-oxidizing-site (Qo-site) by EPR on two-dimensionally ordered samples. Almost identical
The National Academy of Sciences.
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3. Shear-Induced Unfolding of Lysozyme Monitored In Situ
Conformational changes due to externally applied physiochemical parameters, including pH, temperature, solvent composition, and mechanical forces, have been extensively reported for numerous proteins. However, investigations on the effect of fluid shear flow on protein conformation remain inconclusive despite its importance not only in the research of protei
The Biophysical Society.
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4. Polarized Raman spectroscopy of double-stranded RNA from bacteriophage phi6: local Raman tensors of base and backbone vibrations.
Raman tensors for localized vibrations of base (A, U, G, and C), ribose and phosphate groups of double-stranded RNA have been determined from polarized Raman measurements on oriented fibers of the genomic RNA of bacteriophage phi6. Polarized Raman intensities for which electric vectors of both the incident and scattered light are polarized either perpendicul
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5. Modeling of polypeptide chains as C alpha chains, C alpha chains with C beta, and C alpha chains with ellipsoidal lateral chains.
In an effort to reduce the number of degrees of freedom necessary to describe a polypeptide chain we analyze the statistical behavior of polypeptide chains when represented as C alpha chains, C alpha chains with C beta atoms attached, and C alpha chains with rotational ellipsoids as models of side chains. A statistical analysis on a restricted data set of 75