Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Residues defined

The (5 )-enantioselectivity of MeHNL can be explained considering Fig. 1. As shown in the figure, the carbonyl oxygen is hydrogen bonded to SerSO and Thrll. One methyl group of acetone (Cl) is held in position by van der Waals contacts to Leu 149, Thrll and He 12. The side chains of these residues define a... [Pg.151]

Fig. 7.6 The 33-residue fragment of the winter flounder antifreeze protein (AFP), constructed by the conjoining of the Aa amino acid residues defined within the glycine mold , pictured in terms of its 0.001 au isodensity envelope, its van der Waals envelope. This is a view showing the ice-binding motif. It is believed that the AFP strand binds... [Pg.221]

In addition to the value of yfc, graphical tests are useful. The most important of these is the plot of the weighted residuals, defined as... [Pg.183]

When the number of data points is large (i.e. in the single-photon timing technique, or in phase fluorometry when using a large number of modulation frequencies), the autocorrelation function of the residuals, defined as... [Pg.183]

Thoma F, Roller T (1977) Influence of histone HI on chromatin structure. Cell 12 101-107 Thoma F, Roller T, Klug A (1979) Involvement of histone HI in the organization of the nucleosome and of the salt-dependent superstructures of chromatin. J Cell Biol 83 403 27 Turner BM, Birley AJ, Lavender J (1992) Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell 69 375-384... [Pg.28]

Turner, B.M., Birley, A.J., and Lavender, J.S. (1992) Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell 69, 375-384. [Pg.305]

An sp3 carbon must attach to amide nitrogen of previous residue Defined Component 3... [Pg.216]

In practice the error distribution is usually unknown, and the choice can be made an the basis of the empirical curtosis of the residuals defined by... [Pg.210]

Fig. 5. Various parameters of accessibility, twist, and bend plotted vs. sequence number. Part 1 (a) Solvent-accessible area of side chains, (b) Fractional accessibility (referred to full sphere) of backbone carbonyl oxygen and peptide nitrogen. The separate plot for values less than 1% is meant to show that no accessibility was detected for many atoms. The actual nonzero values are not to be taken too literally. Part 2 (c) Backbone angles as normally defined, (d) Angles between sequentially adjacent carbonyl vectors in the backbone plotted between the sequence numbers of the two residues involved. Part 3 (e) Distance in A between the tips, T, of adjacent residues as defined in the text, (f) Distances in A between peptide center, M, and the third sequential peptide center (open circles), and between carbon a and the sixth sequential a-carbon (crosses) plotted opposite the central carbon atom in each case, (g) Angles between lines joining the centers of successive peptide bonds plotted between the residues defining the central bond, (h) Angles between lines joining successive a carbons plotted opposite the central carbon, (Note that the accessibilities were calculated with coordinate set 4 and the other parameters with set 6 see text.)... Fig. 5. Various parameters of accessibility, twist, and bend plotted vs. sequence number. Part 1 (a) Solvent-accessible area of side chains, (b) Fractional accessibility (referred to full sphere) of backbone carbonyl oxygen and peptide nitrogen. The separate plot for values less than 1% is meant to show that no accessibility was detected for many atoms. The actual nonzero values are not to be taken too literally. Part 2 (c) Backbone angles as normally defined, (d) Angles between sequentially adjacent carbonyl vectors in the backbone plotted between the sequence numbers of the two residues involved. Part 3 (e) Distance in A between the tips, T, of adjacent residues as defined in the text, (f) Distances in A between peptide center, M, and the third sequential peptide center (open circles), and between carbon a and the sixth sequential a-carbon (crosses) plotted opposite the central carbon atom in each case, (g) Angles between lines joining the centers of successive peptide bonds plotted between the residues defining the central bond, (h) Angles between lines joining successive a carbons plotted opposite the central carbon, (Note that the accessibilities were calculated with coordinate set 4 and the other parameters with set 6 see text.)...
Step 1. Compute the detection residuals defined in (6.15) then ... [Pg.136]

The system can be considered with one input state (initial charge) and three output states (main-cut 1, off-cut 1, and bottom residue) defined by (B0, xB0), (Dh xDi), (Ri, xRI) and (B2, xB2), respectively. For a mixture with nc components each state is characterised by total amount of material and component mole fractions (nc... [Pg.157]

Fig. 17A (see color insert) shows a ribbon model of the rhodopsin structure indicating the residues assigned to the interface in each helix by a sphere centered on the corresponding of-carbon. Also shown is a sphere on the a-carbon of residue 314, which is located in the interface (see Section III,F). Clearly, these residues define a unique plane of intersection of the molecule with the membrane-aqueous interface. The shaded band in Fig. 17 represents a phospholipid bilayer with a phosphate-phosphate distance of 40 A, the expected thickness of the bilayer in the disk membrane (Saiz and Klein, 2001). The outer interface of the bilayer is positioned so that the polar head groups coincide with the intersection plane defined by the data in Fig. 16. This procedure then fixes the intersection plane of the molecule on the extracellular surface as well. Fig. 17A (see color insert) shows a ribbon model of the rhodopsin structure indicating the residues assigned to the interface in each helix by a sphere centered on the corresponding of-carbon. Also shown is a sphere on the a-carbon of residue 314, which is located in the interface (see Section III,F). Clearly, these residues define a unique plane of intersection of the molecule with the membrane-aqueous interface. The shaded band in Fig. 17 represents a phospholipid bilayer with a phosphate-phosphate distance of 40 A, the expected thickness of the bilayer in the disk membrane (Saiz and Klein, 2001). The outer interface of the bilayer is positioned so that the polar head groups coincide with the intersection plane defined by the data in Fig. 16. This procedure then fixes the intersection plane of the molecule on the extracellular surface as well.
The crystallographic residual E ay The most common form of E ay consists of the crystallographic residual, defined as the sum over the squared differences between the observed ( Fo6s( )l) nd calculated ( f coic( ) ) structure factor amplitudes ... [Pg.261]

Other parvulins also give important structural and mechanistic information. In particular, PinlAt, the Pinl homolog from Arabidopsis thaliana, displays a high degree of similarity with Pinl despite the absence of the Trp-Trp site. In particular, all residues defined as essential in Pinl are represented in PinlAt. In this enzyme, however, binding of the substrate seems to cause the Cys70 side-chain to protrude outside the catalytic site, making it unlikely to interact with the amino acyl proline peptide bond [157]. [Pg.277]

Figure 34 Stereoview of the residues defining the ammonia tunnei in Fd-dependent Synechocystis GitS (1OFE) and crystaiiographic waters (red spheres). Residue side chains are shown as sticks. Coioring C - magenta (centrai domain residues) and green (FMN-binding domain residues), 0-red, N -biue, P-orange, and S-yeiiow. image rendered in PYMOL. Figure 34 Stereoview of the residues defining the ammonia tunnei in Fd-dependent Synechocystis GitS (1OFE) and crystaiiographic waters (red spheres). Residue side chains are shown as sticks. Coioring C - magenta (centrai domain residues) and green (FMN-binding domain residues), 0-red, N -biue, P-orange, and S-yeiiow. image rendered in PYMOL.

See other pages where Residues defined is mentioned: [Pg.53]    [Pg.180]    [Pg.135]    [Pg.298]    [Pg.300]    [Pg.93]    [Pg.128]    [Pg.120]    [Pg.235]    [Pg.97]    [Pg.233]    [Pg.369]    [Pg.777]    [Pg.779]    [Pg.399]    [Pg.132]    [Pg.226]    [Pg.996]    [Pg.132]    [Pg.141]    [Pg.330]    [Pg.87]    [Pg.361]    [Pg.127]    [Pg.126]    [Pg.127]    [Pg.162]    [Pg.182]    [Pg.187]    [Pg.194]    [Pg.213]    [Pg.214]    [Pg.221]    [Pg.532]    [Pg.913]   
See also in sourсe #XX -- [ Pg.372 ]




SEARCH



Residual risk defined

© 2024 chempedia.info