Protein number

Component Mass (mw) Protein Number Mass Size RNA Mass Bases... 

Detection method Number of proteins Number of residues... 

Fig. 19.9 Left nmrDraw-integrated display of the result of a Principal Component Analysis (PCA) for about 100 2D spectra. Numbers in yellow correspond to spectra in which a testing compound does not lead to shift changes of the protein. Numbers in cyan represent spectra whose PCA...

Functional Protein Number of Genes Percentage of Total Genes... 

Protein Number of amino acid residues Protein Number of amino acid residues... 

Figure 5-32 (A) A three-dimensional computer graphics model proposed by Brimacombe et a/.3 11 for the single chain of E. coli 16S ribosomal RNA. The helices are depicted as cylinders, which are all connected. The small dark squares denote the positions of artificially formed RNA-protein crosslinks, marked with the appropriate protein number. For proteins exhibiting more than one crosslink site (e.g., SI7), the sites are denoted A or B, in each case A being the site nearer to the 5 terminus of the 16S RNA. (B) Stereoscopic view of tentative atomic model of 16S RNA in the 30S ribosomal subunit. The viewing direction is different from that in (A). From Mueller and Brimacombe.342 Courtesy of Richard Brimacombe.

Arrangement of components in the E. coli 30S ribosomal particle. In (a) the relative locations of the ribosomal proteins, numbered 1-21, are shown. (Illustration prepared by Dr. Malcolm Capel from data described in M. S. Capel, M. Kjeldguard, D. M. Engelman,. /. Mol. Biol. 200 66-87,... 

Note Mean values, s.d., are activities expressed in milliunits (nmol phosphate released/min per mg protein) number of determinations = 4. 

O. G. Berg. A model for the statistical fluctuations of protein numbers in a microbial population. J. Theoret. Biol., 71 587-603, 1978. 

Protein Approx % of skimmilk protein Number of components 5 Isoionic point Molecular weight0... 

Fig. 11.10 Histogram of c7stallization hits for sparse matrix screens of model proteins. Number of screens tested on each protein are lysosyme (L)=2, glucose isomer-ase (Cl)=2, protease K (PK) = 1, bovine liver catalase (BLC) = 1, xylanase (X) = 2, bacterial primase catalytic core domain (BPC) = 3, bovine pancreas t7psin (BT) = 1, thaumatin (T) = l, mycobacterial RNase (MR)=3.

Fig. 28.1. In a genetic switch, the total state of the system depends on two variables whether the DNA site is occupied or not and the number of copies of the transcription factor. In the left panel, the logarithm of the steady state probability for the occupancy state and protein number is plotted. This probability acts like an effective potential. In the right panel, the effective potential for a charge transfer or two site polaron is plotted as a function of the enviromnent polarization for the two electronic states. The governing time-dependent eqnations for the two problems share many similarities...

Fig. 28.2. The left panel shows the effective potential for a simple gene switch analogous to that shown in Fig. 28.1. AC is a variable that scales with the protein number. gives the value of the number of transcription factor molecules needed (at equilibrium) to give an equal likelihood of the site being occupied or not. The right panel shows the demarcation lines for two-state switch behavior (for large o) and versus one-state averaged behavior for small cu or x )...

Fig. 28.5. The effective potential surfaces for a simple gene switch are shown - h gives the binding rate, f the unbinding rate, and g and g are the synthesis rates when the gene is on or off, respectively. The different diagrams correspond with different sequences of binding/synthesis/unbinding events. The upper plot shows the typical trajectory at high non-adiabaticity. The lowest plot shows the adiabatic case. A churning process gives an enhanced rate of protein number fluctuations in the intermediate weakly non-adiabatic case B...

Table 1. Pairwise Comparisons of the Percent Identity of the Mature Acrosomal Proteins, Number of Synonymous (Ds), and Nonsynonymous (Dn) Substitutions Per...

Proteins Number of subjects Method Glycosylation (%) CV (%) References... 

The MFS is an ancient and diverse set of proteins numbering more than 1000 sequenced membranes that are involved in transporting sugars, metabolites, anions, and drugs. Most MFSs are single-component systems. 

For each protein, number of residues is shown. Helix 1 and 2 are on one side of proteins, and helix 3 and 4 are on the other side of proteins (Rg. 33.3d)... 

Fig. 13.2.6. Model of the hydrogen bridge between Glu 272 (yeast protein numbering) of the bq complex and the carbonyl group of a strobilurin pharmacophore. (Adapted from Refs. [8, 60, 61].) Glyl43 indicates the area of steric repulsion between strobilurins and the resistant Glyl43Ala mutants. The torsion of the pharmacophore relative to the side chain S is adapted from the active, torsionally restricted (+)-enantiomer in Ref [65].

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