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Domains mobility

Orientational restraints, which are derived by paramagnetic labeling of a single domain of a protein, are especially important for the analysis of domain-domain interactions (141). The paramagnetic tag induces anisotropic alignment, which is scaled for the two domains of the protein according to their relative domain mobility. [Pg.1287]

H Kim, D Xia, C-A Yu, J-Z Xia, AM Kachurin, L Zhang, L Yu and J Deisenhofer (1999) Inhibitorbinding changes domain mobility in the iron-sulfur protein of the mitochondrial bcl complex from bovine heart. Proc Nat Acad Sci, USA 95 8026-8033... [Pg.664]

Microdomain size in phase-separated copolymers plays a fundamental role in determining various macroscopic physical properties in the solid state. The difference in segmental mobility between the hard and soft domains governs the physical properties of microphase-separated polyurethane elastomers [7]. In this respect, the development of structure-property relations at the molecular level which relate directly to macroscopic behavior is the focus of this sub-section. One can exploit the well-documented difference between domain mobility [7-10] and the i3C NMR chemical shift distinction between the 0 .H2 resonances in the hard and soft segments to probe the microdomain morphology of polyether-... [Pg.122]

Theoretical models of the film viscosity lead to values about 10 times smaller than those often observed [113, 114]. It may be that the experimental phenomenology is not that supposed in derivations such as those of Eqs. rV-20 and IV-22. Alternatively, it may be that virtually all of the measured surface viscosity is developed in the substrate through its interactions with the film (note Fig. IV-3). Recent hydrodynamic calculations of shape transitions in lipid domains by Stone and McConnell indicate that the transition rate depends only on the subphase viscosity [115]. Brownian motion of lipid monolayer domains also follow a fluid mechanical model wherein the mobility is independent of film viscosity but depends on the viscosity of the subphase [116]. This contrasts with the supposition that there is little coupling between the monolayer and the subphase [117] complete explanation of the film viscosity remains unresolved. [Pg.120]

By linking the chain ends of different molecules they form a type of network structure as long as the domains remain glassy. As the polymer is heated above the of the domain polymer block the domain molecules become mobile and on application of a stress the material flows like a thermoplastic. On cooling, new domains will be formed, thus regenerating the elastic state. [Pg.298]

Fig. 22. Nomialized pull-off energy measured for polyethylene-polyethylene contact measured using the SFA. (a) P versus rate of crack propagation for PE-PE contact. Change in the rate of separation does not seem to affect the measured pull-off force, (b) Normalized pull-off energy, Pn as a function of contact time for PE-PE contact. At shorter contact times, P does not significantly depend on contact time. However, as the surfaces remain in contact for long times, the pull-off energy increases with time. In seinicrystalline PE, the crystalline domains act as physical crosslinks for the relatively mobile amorphous domains. These amorphous domains can interdiffuse across the interface and thereby increase the adhesion of the interface. This time dependence of the adhesion strength is different from viscoelastic behavior in the sense that it is independent of rate of crack propagation. Fig. 22. Nomialized pull-off energy measured for polyethylene-polyethylene contact measured using the SFA. (a) P versus rate of crack propagation for PE-PE contact. Change in the rate of separation does not seem to affect the measured pull-off force, (b) Normalized pull-off energy, Pn as a function of contact time for PE-PE contact. At shorter contact times, P does not significantly depend on contact time. However, as the surfaces remain in contact for long times, the pull-off energy increases with time. In seinicrystalline PE, the crystalline domains act as physical crosslinks for the relatively mobile amorphous domains. These amorphous domains can interdiffuse across the interface and thereby increase the adhesion of the interface. This time dependence of the adhesion strength is different from viscoelastic behavior in the sense that it is independent of rate of crack propagation.
Today, the use of CHIRBASE as a tool in aiding the chemist in the identification of appropriate CSPs has produced impressive and valuable results. Although recent developments diminish the need for domain expertise, today the user must possess a certain level of knowledge of analytical chemistry and chiral chromatography. Nevertheless, further refinements will notably reduce this required level of expertise. Part of this effort will include the design of an expert system which will provide rule sets for each CSP in a given sample search context. The expert system will also be able to query the user about the specific requisites for each sample (scale, solubility, etc.) and generate rules which will indicate a ranked list of CSPs as well their most suitable experimental conditions (mobile phase, temperature, pH, etc.). [Pg.122]

In contrast to PEG-1000, the ESR-spectra obtained for labelled grafted PEO-oligomers (N = 1-9) were reported to differ strongly from that for N = 23 and exhibited only slowly moving labels. As the fine width of the fast domain spectrum depends on the mobility of the label, it can be concluded that the tails for N = 23 must consist of at least 4-9 repeated units. It appears that some tails are rather long. [Pg.141]

AChE-R (in purple) Naturally rare, stress-induced variant, which lacks a hydrophobic domain and is incapable of binding to ColQ or PRiMA. Therefore, it remains soluble, and its secreted form shows greater mobility than AChE-S. AChE-R can intra-cellularly interact through its C-terminal tail with the Protein Kinase C Receptor RACK1, a scaffold protein which modifies multiple cellular processes. [Pg.360]

The HMG (high mobility group) box is a DNA-binding domain found in several transcription factors, that can in some cases bend DNA. Some members of this protein family recognize a unique DNA sequence, whereas others bind to a common DNA conformation. [Pg.596]

The VACM-1 receptor is a membrane-associated protein with a single putative transmembrane domain that binds selectively AVP (XD — 2 nM), but cannot discriminate between VXR and V2R analogues. It is expressed in endothelial and medullary collecting duct cells and upon stimulation by AVP. It induces a mobilization of cytosolic-free Ca2+, decreases cAMP production and inhibits cellular growth via MAPK phosphorylation and p53 expression. The mechanism of action and physiological functions of this new receptor are not well understood, but it seems to participate in the regulation of AVP induced signal transduction pathways or of a yet unidentified peptide. [Pg.1276]


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See also in sourсe #XX -- [ Pg.514 ]




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