970 resultados para Amino-acid residues


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A novel racemization observed in the Vitamin B6-amino acid Schiff base complexes, aquo (5'-phosphopyridoxylidene-l-tyrosinato) copper(II) and aquo (5'-phosphopyridoxylidene-l-phenylalaninato) copper(II) is described. The racemization taking place in solution under mild acidic conditions (pH 5-6) was confirmed by CD studies and the products were characterized by single crystal X-ray diffraction. The structures of both complexes show almost parallel orientation of the aromatic side chain and the pyridoxal II-system. The activation of the αCsingle bondH group due to the intermolecular II- interaction is probably the reason for the unusual racemization observed.

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Plant seeds contain a large number of protease inhibitors of animal, fungal, and bacterial origin. One of the well-studied families of these inhibitors is the Bowman-Birk family(BBI). The BBIs from dicotyledonous seeds are 8K, double-headed proteins. In contrast, the 8K inhibitors from monocotyledonous seeds are single headed. Monocots also have a 16K, double-headed inhibitor. We have determined the primary structure of a Bowman-Birk inhibitor from a dicot, horsegram, by sequential edman analysis of the intact protein and peptides derived from enzymatic and chemical cleavage. The 76-residue-long inhibitor is very similar to that ofMacrotyloma axillare. An analysis of this inhibitor along with 26 other Bowman-Birk inhibitor domains (MW 8K) available in the SWISSPROT databank revealed that the proteins from monocots and dicots belong to related but distinct families. Inhibitors from monocots show larger variation in sequence. Sequence comparison shows that a crucial disulphide which connects the amino and carboxy termini of the active site loop is lost in monocots. The loss of a reactive site in monocots seems to be correlated to this. However, it appears that this disulphide is not absolutely essential for retention of inhibitory function. Our analysis suggests that gene duplication leading to a 16K inhibitor in monocots has occurred, probably after the divergence of monocots and dicots, and also after the loss of second reactive site in monocots.

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Mycobacterium leprae recA harbors an in-frame insertion sequence that encodes an intein homing endonuclease (PI-MleI). Most inteins (intein endonucleases) possess two conserved LAGLIDADG (DOD) motifs at their ctive center. A common feature of LAGLIDADG-type homing endonucleases is that they recognize and cleave the same or very similar DNA sequences. However, PI-MleI is distinctive from other members of the family of LAGLIDADG-type HEases for its modular structure with functionally separable domains for DNA-binding and cleavage, each with distinct sequence preferences. Sequence alignment analyses of PI-MleI revealed three putative LAGLIDADG motifs; however, there is conflicting bioinformatics data in regard to their identity and specific location within the intein polypeptide. To resolve this conflict and to determine the active-site residues essential for DNA target site recognition and double-stranded DNA cleavage, we performed site-directed mutagenesis of presumptive catalytic residues in the LAGLIDADG motifs. Analysis of target DNA recognition and kinetic parameters of the wild-type PI-MleI and its variants disclosed that the two amino acid residues, Asp(122) (in Block C) and Asp(193) (in functional Block E), are crucial to the double-stranded DNA endonuclease activity, whereas Asp(218) (in pseudo-Block E) is not. However, despite the reduced catalytic activity, the PI-MleI variants, like the wild-type PI-MleI, generated a footprint of the same length around the insertion site. The D122T variant showed significantly reduced catalytic activity, and D122A and D193A mutations although failed to affect their DNA-binding affinities, but abolished the double-stranded DNA cleavage activity. On the other hand, D122C variant showed approximately twofold higher double-stranded DNA cleavage activity, compared with the wild-type PI-MleI. These results provide compelling evidence that Asp(122) and Asp(193) in DOD motif I and II, respectively, are bona fide active-site residues essential for DNA cleavage activity. The implications of these results are discussed in this report.

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Four new 5-aminoisophthalates of cobalt and nickel have been prepared employing hydro/solvothermal methods: [Co2(C8H5NO4)2(C4H4N2)(H2O)2]·3H2O (I), [Ni2(C8H5NO4)2(C4H4N2)(H2O)2]·3H2O (II), [Co2(H2O)(μ3-OH)2(C8H5NO4)] (III), and [Ni2(H2O)(μ3-OH)2(C8H5NO4)] (IV). Compounds I and II are isostructural, having anion-deficient CdCl2 related layers bridged by a pyrazine ligand, giving rise to a bilayer arrangement. Compounds III and IV have one-dimensional M−O(H)−M chains connected by the 5-aminoisophthalate units forming a three-dimensional structure. The coordinated as well as the lattice water molecules of I and II could be removed and inserted by simple heating−cooling cycles under the atmospheric conditions. The removal of the coordinated water molecule is accompanied by changes in the coordination environment around the M2+ (M = Co, Ni) and color of the samples (purple to blue, Co; green to dark yellow, Ni). This change has been examined by a variety of techniques that include in situ single crystal to single crystal transformation studies and in situ IR and UV−vis spectroscopic studies. Magnetic studies indicate antiferromagnetic behavior in I and II, a field-induced magnetism in III, and a canted antiferromagnetic behavior in IV.

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Understanding the key factors that influence the interaction preferences of amino acids in the folding of proteins have remained a challenge. Here we present a knowledge-based approach for determining the effective interactions between amino acids based on amino acid type, their secondary structure, and the contact based environment that they find themselves in the native state structure as measured by their number of neighbors. We find that the optimal information is approximately encoded in a 60 x 60 matrix describing the 20 types of amino acids in three distinct secondary structures (helix, beta strand, and loop). We carry out a clustering scheme to understand the similarity between these interactions and to elucidate a nonredundant set. We demonstrate that the inferred energy parameters can be used for assessing the fit of a given sequence into a putative native state structure.

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This paper reports the observation of a reversible disassembly process for a previously reported octanuclear Cu(II) complex with imidazole. To identify the factors responsible for the process, five Cu(II) complexes of different nuclearity with different amino acid-derived tetradentate ligands were structurally characterized. The results show that the coordination geometry preference of Cu(II), the tendency of imidazole to act as in-plane ligand, and H-bonding played important role in the formation and disassembly of the octanuclear complex. A general scheme describing the effect of different amino acid side arms, solvents, and exogenous ligands on the nuclearity of the Cu(II) complexes has been presented. The crystals of the complexes also showed formation of multifaceted networks in the resulting complexes.

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The use of stereochemically constrained amino acids permits the design of short peptides as models for protein secondary structures. Amino acid residues that are restrained to a limited range of backbone torsion angles (ϕ-ψ) may be used as folding nuclei in the design of helices and β-hairpins. α-Amino-isobutyric acid (Aib) and related Cαα dialkylated residues are strong promoters of helix formation, as exemplified by a large body of experimentally determined structures of helical peptides. DPro-Xxx sequences strongly favor type II’ turn conformations, which serve to nucleate registered β-hairpin formation. Appropriately positioned DPro-Xxx segments may be used to nucleate the formation of multistranded antiparallel β-sheet structures. Mixed (α/β) secondary structures can be generated by linking rigid modules of helices and β-hairpins. The approach of using stereochemically constrained residues promotes folding by limiting the local structural space at specific residues. Several aspects of secondary structure design are outlined in this chapter, along with commonly used methods of spectroscopic characterization.

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Determination of the protein content and lysine levels of a number of nonhybrid varieties of grain sorghum indicates large variations in the protein content. Statistical analysis of data on amounts of lysine shows that a negative correlation exists between per cent lysine in the protein and per cent protein in the seed. The proportion of various protein fractions in endosperm of five varieties of grain sorghum of both low- and high-protein type has been determined. Results show that prolamine and glutelin are the principal protein fractions, and increased protein levels in sorghum varieties are correlated with an increase mainly in the prolamine fraction. Nine high- and low-protein varieties of grain sorghum have been analyzed for their amino acid composition by ion exchange procedures. One of the high-protein genetic varieties of sorghum has a high concentration of lysine in the seed. Amino acid composition of the protein fractions of two varieties is also reported. These data permit an evaluation of the nutritional quality of sorghum protein and factors that influence the quality of the protein.

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Abstract—β-N-Oxalyl-l-α,β-diaminopropionic acid (ODAP), the toxin isolated from the seeds of Luthyrus sativus produces head retraction, tremors and convulsions when injected into a variety of experimental animals. In 12-day-old rats, it has been found that the convulsive behaviour is accompanied by profound biochemical changes in the brain. The brain homogenates prepared from ODAP injected animals show a higher rate of respiration. There is a decrease in the brain glucose, glycogen, ATP, phosphocreatine and acetylcholine levels of the convulsing animals. The inorganic phosphate, lactic acid and acetylcholineesterase levels increase. These results establish that ODAP is a typical convulsant.

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1. The polarographic behaviour of amino-acid complexes of zinc has been studied using seven amino acids as complexing agents. 2. The effect of varying the pH of the base solution and the concentration of amino-acid anion on the polarographic behaviour of zinc in these solutions have indi cated the formation of twelve amino-acid complexes. The stability constants could not be calculated due to the irreversible nature of the waves. 3. The effect of sodium hydroxide, sodium carbonate, and ammonia on the polarographic behaviour of zinc has been investigated. The results can be interpreted as due to the formation of mixed complexes in many systems. 4. Amino-acid base solutions have been found to be suitable for the polarographic estimation of zinc.

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1. A detailed polarographic study of cadmium has been made employing glycine, α-alanine, β-alanine, valine, aspartic acid, glutamic acid and asparagine as complexing agents at various pH values. The effect of incorporating sodium hydroxide, sodium carbonate and ammonium nitrate + ammonium hydroxide, on the polarographic behaviour of amino acid complexes of cadmium has also been investigated. 2. The reduction process has been found to be reversible in all systems. 3. The small shifts in the half-wave potentials noticed due to increase in the concentration of sodium hydroxide and sodium carbonate in presence of amino acids have been explained on the basis of formation of mixtures of pure and mixed amino acid complexes of cadmium. Mixed complexes have also been noticed in presence of ammonium hydroxide and ammonium nitrate and amino acids. 4. Polarographic evidence has been obtained for the formation of over 30 pure and mixed complexes. The dissociation constant Kd, the Δ F° value for the dissociation, and standard potential value for the formation, of each complex have been computed. 5. It has been found that cadmium can be polarographically estimated in amino acid solutions.

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1. The polarographic behaviour of glycine, α-alanine, β-alanine, valine, aspartic acid, glutamic acid and asparagine complexes of lead has been studied at various pH values and in presence of (1) NaOH, (2) Na2CO3 and (3) NH4 NO3+NH4OH. All the polarographic waves have been found to be reversible. 2. Experiments conducted on the effect of variation of pH, i.e., 7amino-acid have indicated the formation of Pb A and Pb A2. The data have been analysed employing the equations developed by DeFord and Hume as modified by McKenzie and Mellor. 3. Only pure complexes are produced below pH 11·2 in the case of aspartic acid, glutamic acid and glycine, while mono hydroxy complexes are produced in α-alanine, valine and asparagine systems. 4. It has been found that no mixed hydroxy and mixed ammonia complexes are produced in presence of sodium hydroxide and ammonia-ammonium nitrate, respectively. However evidence is obtained for the formation of mixed carbonate complexes in glycine and aspartic acid systems in presence of sodium carbonate. 5. Thermodynamic data have been calculated from polarographic measurements for 18 complexes. 6. The suitability of incorporating amino acids in base solutions for the polarographic estimation of lead has been tested.