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Plus domains

Therefore the second-order derivative of/ appearing in the original form of / is replaced by a term involving first-order derivatives of w and/plus a boundary term. The boundary terms are, normally, cancelled out through the assembly of the elemental stiffness equations over the common nodes on the shared interior element sides and only appear on the outside boundaries of the solution domain. However, as is shown later in this chapter, the appropriate treatment of these integrals along the outside boundaries of the flow domain depends on the prescribed boundary conditions. [Pg.78]

In such openings, bidirectional flow driven by temperature differences between the two rooms can occur. If a total pressure (static pressure plus dynamic pressure) is specified, this phenomenon can be accounted for. For higher accuracy in the neighborhood of this opening, it is, however, recommended to expand the calculation domain beyond this opening. [Pg.1037]

Motor proteins move along MTs in an ATP-dependent manner. Members of the superfamily of kinesin motors move only to the plus ends and dynein motors only to the minus ends. The respective motor domains are linked via adaptor proteins to their cargoes. The binding activity of the motors to MTs is regulated by kinases and phosphatases. When motors are immobilized at their cargo-binding area, they can move MTs. [Pg.415]

Peptidases have been classified by the MEROPS system since 1993 [2], which has been available viatheMEROPS database since 1996 [3]. The classification is based on sequence and structural similarities. Because peptidases are often multidomain proteins, only the domain directly involved in catalysis, and which beais the active site residues, is used in comparisons. This domain is known as the peptidase unit. Peptidases with statistically significant peptidase unit sequence similarities are included in the same family. To date 186 families of peptidase have been detected. Examples from 86 of these families are known in humans. A family is named from a letter representing the catalytic type ( A for aspartic, G for glutamic, M for metallo, C for cysteine, S for serine and T for threonine) plus a number. Examples of family names are shown in Table 1. There are 53 families of metallopeptidases (24 in human), 14 of aspartic peptidases (three of which are found in human), 62 of cysteine peptidases (19 in human), 42 of serine peptidases (17 in human), four of threonine peptidases (three in human), one of ghitamicpeptidases and nine families for which the catalytic type is unknown (one in human). It should be noted that within a family not all of the members will be peptidases. Usually non-peptidase homologues are a minority and can be easily detected because not all of the active site residues are conserved. [Pg.877]

FIG. 4 Onion model of spherical water-containing reversed micelles. Solvent molecules are not represented. A, surfactant alkyl chain domain B, head group plus hydration water domain C, hulk water domain. (For water-containing AOT-reversed micelles, the approximate thickness of layer A is 1.5 nm, of layer B is 0.4 nm, whereas the radius of C is given hy the equation r = 0.17R nm.)... [Pg.481]

Figure 7.6 STM images (100 x 100) A2 of Pt(lll) under different catalytic conditions 7 (a) 20 mTorr H2 (b) 20mTorr H2 and 20mTorr C2H4 (c) 20mTorr H2 plus 20mTorr C2H4 and 2.5mTorr CO(g). The CO added induced the formation of a ( /l9 x /l9) R23.4° structure in (c). In (d) are shown two rotational domains of the /T9 structure. (Reproduced from Ref. 7). Figure 7.6 STM images (100 x 100) A2 of Pt(lll) under different catalytic conditions 7 (a) 20 mTorr H2 (b) 20mTorr H2 and 20mTorr C2H4 (c) 20mTorr H2 plus 20mTorr C2H4 and 2.5mTorr CO(g). The CO added induced the formation of a ( /l9 x /l9) R23.4° structure in (c). In (d) are shown two rotational domains of the /T9 structure. (Reproduced from Ref. 7).
Performance data Two moisture monitoring systems were installed, one at Disposal Area A and one at Disposal Area AB plus in May and November 1999, respectively. Each monitoring system has two stacks of time domain reflectometry probes that measure soil moisture at 24-in. intervals to a maximum depth of 78 in., and a station for collecting weather data. Based on nearly 3 years of data, there is generally <5% change in the relative volumetric... [Pg.1082]

Limit in the signal domain, estimated from the average blank plus its uncertainty, generally according... [Pg.312]

Amorphous poly(methylene) plus aliphatics in domains, sample weight %... [Pg.130]

In conclusion, the goal of predictive process modelling has not yet been achieved due to the interference of chemical reactions with mass transport. All polycondensation models and process simulators available in the public domain, such as Polymer Plus from AspenTech or Predici from CIT, as well as in-house polycondensation models from engineering companies and producers, cannot be used for design or scale-up successfully without the use of fitting parameters. [Pg.89]

Fig. 5. Schematic representation of the domain structure of albumin, the position of the disulfide loops, and the fragments of the molecule that have been isolated. Included in the figure are the cleavage methods used to obtain the fragments plus the regions to which the restricted antibody populations used in these experiments are directed. Reprinted, with permission, from Teale and Benjamin (1976). Copyright by the American Society of Biological Chemists, Inc. Fig. 5. Schematic representation of the domain structure of albumin, the position of the disulfide loops, and the fragments of the molecule that have been isolated. Included in the figure are the cleavage methods used to obtain the fragments plus the regions to which the restricted antibody populations used in these experiments are directed. Reprinted, with permission, from Teale and Benjamin (1976). Copyright by the American Society of Biological Chemists, Inc.
Fig. 2. The binding of Cu s in ascorbate oxidase. A section of the polypeptide (plus side chains), and position of the type 1 Cu in a plastocyanin like domain (to the right) are shown. The type 3 Cu s are attached at what corresponds to the remote site. Residues HisS07 and CysSOS are analogous to Tyr83 and Cys84 in plastocyanin... Fig. 2. The binding of Cu s in ascorbate oxidase. A section of the polypeptide (plus side chains), and position of the type 1 Cu in a plastocyanin like domain (to the right) are shown. The type 3 Cu s are attached at what corresponds to the remote site. Residues HisS07 and CysSOS are analogous to Tyr83 and Cys84 in plastocyanin...

See other pages where Plus domains is mentioned: [Pg.179]    [Pg.157]    [Pg.1962]    [Pg.179]    [Pg.157]    [Pg.1962]    [Pg.555]    [Pg.132]    [Pg.195]    [Pg.175]    [Pg.159]    [Pg.324]    [Pg.327]    [Pg.297]    [Pg.231]    [Pg.56]    [Pg.345]    [Pg.279]    [Pg.58]    [Pg.63]    [Pg.528]    [Pg.117]    [Pg.135]    [Pg.107]    [Pg.326]    [Pg.145]    [Pg.340]    [Pg.592]    [Pg.84]    [Pg.246]    [Pg.313]    [Pg.275]    [Pg.211]    [Pg.170]    [Pg.199]    [Pg.249]    [Pg.510]    [Pg.331]    [Pg.136]    [Pg.341]   
See also in sourсe #XX -- [ Pg.157 ]




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