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Protein nucleotides

Although simple solutions can be examined by these electrospray techniques, often for a single substance dissolved in a solvent, straightforward evaporation of the solvent outside the mass spectrometer with separate insertion of the sample is sufficient. This situation is not true for all substances. Peptides, proteins, nucleotides, sugars, carbohydrates, mass organometallics, and many... [Pg.58]

As a rule of thumb, one can say that the efficiency of separation of mixtures and the simplicity of operating and maintaining apparatus are much greater for GC than for LC. Hence, other things being equal, GC is most often the technique of first choice and can be used with a very wide variety of compound types. However, for nonvolatile or thermally labile substances like peptides, proteins, nucleotides, sugars, carbohydrates, and many organometallics, GC may be ruled out completely... [Pg.251]

The macromolecules of cells are built of units—amino acids in proteins, nucleotides in nucleic acids, and carbohydrates in polysaccharides—that have structural polarity. That is, these molecules are not symmetrical, and so they can be thought of as having a head and a tail. Polymerization of these units to form macromolecules occurs by head-to-tail linear connections. Because of this, the polymer also has a head and a tail, and hence, the macromolecule has a sense or direction to its structure (Figure 1.9). [Pg.13]

The kinetics of feedback inhibition may be competitive, noncompetitive, pattially competitive, ot mixed. Feedback inhibitots, which frequently ate the small molecule building blocks of mactomolecules (eg, amino acids for proteins, nucleotides fot nucleic acids), typically inhibit the fitst committed step in a particulat biosynthetic sequence. A much-studied example is inhibition of bacterial aspattate ttanscatbamoylase by CTP (see below and Chaptet 34). [Pg.75]

These basic concepts are followed by a section on the structure of the important biomolecules (pp. 34-87). This part of the book is arranged according to the different classes of metabolites. It discusses carbohydrates, lipids, amino acids, peptides and proteins, nucleotides, and nucleic acids. [Pg.1]

Brakoulias A, Jackson RM (2004) Towards a structural classification of phosphate binding sites in protein-nucleotide complexes an automated all-against-all structural comparison using geometric matching. Proteins Struct Funct Bioinformatics 56 250-260... [Pg.164]

Experimental 3hJ(P,N) couplings across N-H-O-P and 2hJ(P, H) across both N-H-O-P and O-H-O-P hydrogen bonds in protein nucleotide complexes were first reported independently by Riiterjans et al.135 and by Mishima et al.136 For instance, these authors measured the absolute values of 3hJ(P,N) = 4.44 0.06 and 2hJ(P,H) = 3.9 0.8 Hz between Ala 18 and the a-phosphate in wild-type Ras.GDP. Observations made by Mishima et al.136 led them to suggest that 3hJ(P,N) couplings are sensitive to the linear... [Pg.204]

The further biosynthetic pathways from 3-phos-phoglycerate to the myriad amino acids, nucleotides, lipids, and miscellaneous compounds found in cells are complex and numerous. However, the basic features are relatively simple. Figure 17-11 indicates the origins of many substances including the 20 amino acids present in proteins, nucleotides, and lipids. Among the additional key biosynthetic precursors that can be identified from this chart are glucose 6-phosphate, pyruvate, oxaloacetate, acetyl-CoA, 2-oxoglutarate, and succinyl-CoA. [Pg.973]

In theory, if the net charge, q, on a molecule is known, it should be possible to measure / and obtain information about the hydrodynamic size and shape of that molecule by investigating its mobility in an electric field. Attempts to define /by electrophoresis have not been successful, primarily because Equation 4.3 does not adequately describe the electrophoretic process. Important factors that are not accounted for in the equation are interaction of migrating molecules with the support medium and shielding of the molecules by buffer ions. This means that electrophoresis is not useful for describing specific details about the shape of a molecule. Instead, it has been applied to the analysis of purity and size of macromolecules. Each molecule in a mixture is expected to have a unique charge and size, and its mobility in an electric field will therefore be unique. This expectation forms the basis for analysis and separation by all electrophoretic methods. The technique is especially useful for the analysis of amino acids, peptides, proteins, nucleotides, nucleic acids, and other charged molecules. [Pg.112]

Specific interactions between three different repressors and their operator binding sites. Only half the operator binding site is shown because identical contacts are made with the other half. The numbers associated with the amino acid side chains refer to the distance of amino acids from the amino-terminal end of the protein. Nucleotides are numbered from the central dyad at the operator, (a) The 434 phage repressor (b) The A repressor, (c) The trp repressor. (Source Adapted from T. Steitz, Q. Rev. Biophys. 23 236, 1990.)... [Pg.792]

Bruskov, V. I., and Poltev, V. I. (1979). On molecular mechanisms of nucleic acid synthesis. Fidelity aspects 2. Contribution of protein-nucleotide recognition. J. Theor. Biol. 78, 29-41. [Pg.432]

The angular and distance information provided by the lanthanide induced shift has found widespread application from the determination of solution structures of Ln chelates [18,19] to gaining structural information on proteins, nucleotides and amino acids [19], More recently anion binding to coordinatively unsaturated lanthanide complexes has been effectively signalled as the observed lanthanide induced shift has been directly correlated to the nature of the donor atom in the axial position [8,20,21], It is the polarisability of the axial donor that ranks the second order crystal field coefficient, B02, and hence determines the magnitude of the observed shift. Values of the mean shift of the four most-shifted axial protons of the 12-Nq ring for [Yb.la]3+ are collated in Table 2. [Pg.125]

Amino acids link together linearly to form proteins, nucleotides link linearly to form RNA and DNA, and sugars link in a more complicated way to form complex carbohydrates. The specific sequence in which these units link together to form the final polymeric macromolecule is called its primary structure. In a way that is still very ill-understood, the primary structure ultimately controls the macromolecule s three-dimensional structure and thereby largely determines its function. There is therefore great interest in analyzing primary structural information in order to detect similarities and relationships between macromolecules. However, as we shall see later, although similar primary structures imply similar three-dimensional structures, it is possible for three-dimensional structures to resemble each other without any sequence similarity. [Pg.76]

Wash the column four times, each wash containing 4 CV of RNA column wash buffer, to remove excess protein, nucleotides and RNA abortive transcription products. [Pg.15]

Essential amino acids are those not synthesized by the organism and are required by animal cells in culture. These include specific amino acids such as cysteine and tyrosine but the requirement varies between cell lines. Amino acids are necessary for protein, nucleotide, and lipid synthesis and, in addition, may be used as an energy source. [Pg.116]

Nucleoprotein nucleic acid (+ proteins) nucleotides nucleosides (+ phosphate ion)... [Pg.55]

Chapters 1 through 21 cover the topics that most instructors will include in their courses, with the possible exception of Chapter 15. The remaining chapters offer a choice for the last part of the course. They include chapters on pericyclic reactions, synthesis, and polymers. The chapters on the more biochemical topics—carbohydrates, amino acids and proteins, nucleotides and nucleic acids, and other natural products— concentrate on the organic chemistry of these important biomolecules. [Pg.1326]

The general scheme for the degradation of nucleic acids has much in common with that of proteins. Nucleotides are produced by hydrolysis of both dietary and endogenous nucleic acids. The endogenous (cellular) polynucleotides are broken down in lysosomes. DNA is not normally turned over rapidly, except after cell death and during DNA repair. RNA is turned over in much the same way as protein. The enzymes involved are the nucleases deoxyribonucleases and ribonucleases hydrolyze DNA and RNA, respectively, to oligonucleotides which can be further hydrolyzed (Fig. 15-18), so eventually purines and pyrimidines are formed. [Pg.446]

Nucleotide binding sites in proteins can be identified by treating the protein-nucleotide complex with periodate, which cleaves ribonucleotides into highly reactive dialdehydes these are able to couple in a Schiff condensation reaction with the c-amino group of any neighbouring lysine residues (Easterbrook-Smith et al. 1976) (Figure 5-7). This coupling is reversible, but it can be made permanent by reduction with NaBH.. ... [Pg.177]

Figure 5-7. Affinity labelling of nucleotide bind- hyde analogue. These groups react with accessible ing proteins. Nucleotides bound to protein are lysine residues in the region ofthe nucleotide bind-treated with periodate, which cleaves the vicinal ing site to form a Schiffbase adduct this can be diol groups to generate a highly reactive dialde- stabilised by reduction with NaHB4. Figure 5-7. Affinity labelling of nucleotide bind- hyde analogue. These groups react with accessible ing proteins. Nucleotides bound to protein are lysine residues in the region ofthe nucleotide bind-treated with periodate, which cleaves the vicinal ing site to form a Schiffbase adduct this can be diol groups to generate a highly reactive dialde- stabilised by reduction with NaHB4.

See other pages where Protein nucleotides is mentioned: [Pg.68]    [Pg.189]    [Pg.21]    [Pg.351]    [Pg.217]    [Pg.257]    [Pg.418]    [Pg.419]    [Pg.31]    [Pg.219]    [Pg.416]    [Pg.277]    [Pg.60]    [Pg.205]    [Pg.13]    [Pg.16]    [Pg.165]    [Pg.165]    [Pg.9]    [Pg.159]    [Pg.168]    [Pg.494]    [Pg.37]    [Pg.232]    [Pg.272]    [Pg.115]    [Pg.411]    [Pg.351]    [Pg.323]    [Pg.324]   
See also in sourсe #XX -- [ Pg.195 ]




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Application to Proteins and Nucleotide Base Stacks

Cyclic nucleotide-dependent protein

Cyclic nucleotide-dependent protein activation

Cyclic nucleotide-dependent protein kinases

Guanine Nucleotide Exchange Factors (GEFs) in Signal Transduction via Ras Proteins

Guanine nucleotide binding regulatory protein

Guanine nucleotide protein-coupled receptor

Guanine nucleotide regulatory protein

Guanine nucleotide regulatory protein activation

Guanine nucleotide release proteins

Guanine nucleotide-binding proteins

Guanine nucleotide-releasing protein

Guanosine nucleotide regulatory protein

Guanosine nucleotide-binding proteins

Guanosine nucleotide-binding proteins G-protein)

Guanyl nucleotide-binding protein

Iron proteins nucleotides, interaction with

Molecular Interactions of LLCs with Proteins and Nucleotides

Nucleotide binding proteins, iron protein

Nucleotide correlation with protein

Nucleotide hydrolysis, coupling with proteins

Nucleotide-binding proteins

Nucleotide-protein interactions

Nucleotide/protein sets

Protein and Nucleotide Database Group

Protein kinase cyclic-nucleotide-independent

Protein kinase nucleotide-dependent effects

Protein nucleotide-binding domain

Protein sequencing nucleotides compared

Pyridine nucleotides protein binding

Seven-transmembrane domain receptors nucleotide-binding proteins

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