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The transfer of energy perturbations within protein structure is an important phenomenon in many biological processes. In particular, the transfer of energy perturbations within a molecule in the absence of electron transfer is critical to the understanding of such processes as signaling involving receptors, channels, and enzymes among others, and to the design and development of relevant conducting materials. In this work, we have proposed a mechanism to explain this nonradiative, nonelectron energy transfer based on the π-orbital interactions of aromatic amino acids. Additionally, some theoretical background and possible computational approaches are presented as support for the proposal. [ABSTRACT FROM AUTHOR]

We are reporting computational studies of several genotyped strains of astrovirus isolated in Colombia which we have genotyped using the 348-bp segment located between nucleotides 258 and 606 close to the amino terminal region of the complete ORF 2. By biocomputational techniques this 348-bp segment from the different strains was translated into an amino acid sequence. The sequences were aligned and compared in order to build a dendrogram. Our results show that the 348 bp and the 116 amino acid peptides cluster in a very conservative way, showing slight genetic variations between them. This slight sequence variability does not allow us to identify common amino acid substitution patterns shared by all members of each HAstV specific type, thus suggesting that antigenic epitopes are probably located outside the 116 peptide fragment of this capsid protein. These results show that there is little recombination among different regions of the ORF2, thus suggesting that this genotyping method should continue to be useful for serotyping HAstV isolates. [ABSTRACT FROM AUTHOR]

Objective. To propose a methodology that identifies the NR2B subunit through the use of conantokin G, as well as an adequate extraction of the NR2B subunit. Materials and methods, Two methodologies were tested for the extraction of the NR2B subunit of the adult rat, the first one sought the extraction of the subunit through a membrane by using sodium deoxicolate; and the second, guaranteed the solubilization and elimination of cytoplasmic proteins, in order to later extract the subunit through the use of the same detergent from the pellet resulting from the centrifugation of the obtained extract. Additionally, the conantokin G was biotynilated in order to evaluate its efficiency to identify the subunit and to compare the results obtained from traditional methodologies such as DOT-BLOT, WESTERN-BLOT, ELISA and Immunohistochemical. Results. The second methodology showed a greater extraction of NR2B, thus it was chosen for the subsequent extracts. The identification tests with biotynilated conantokin showed interference in recognition, thus, it was necessary identify the subunit NR2B through the use of the polyclonal antibodies mentioned in the tests. Conclusions, An impediment of esteric character is proposed in marking the conantokin with the biotin, which does not favor the interaction of this peptide with the subunit. [ABSTRACT FROM AUTHOR]

The recombinant human iduronate 2-sulfate sulfatase (hrIDS) was transiently and functionally active expressed in E. coli K12. The enzyme activity (crude extract) at 100 ml and 400 ml oscillated between 0.25 and 10.58 nmol h-1 mg-1. The wide Western-blot peptide profile suggest that hrIDS is proteolitically processed "randomly" which agrees with the ultrafiltration assay in which the hrIDS activity was found in all fractions (<30kDa, 30-100kDa and >100kDa). No glycation sites were found by computer analysis of the hIDS sequence; discarding the possibility of marks for glycation and proteolytic processing. [ABSTRACT FROM AUTHOR]

Objective, To obtain IgY antibodies against synthetic peptides of NR3A and NR3B subunits of the rat NMDA receptor, to recognize and follow the expression of these subunits in rat brain extract at different ages. Materials and methods. By using Entrez data base and ClustalW-PBIL program for sequence alignment two peptides against NR3A and NR3B subunits of the NMDA receptor were designed, Once synthesized by SSPS-fmoc method, peptides were then inoculated into 16-week-old chickens (Gallus gallus, var. Hy Line Brown). After 57 days specific IgY was purified and confronted with postnatal and adult rat brain extract. Results. Both subunits NR3A and NR3B were detected and their expression was related to rat age. The level of expression of NR3A was higher in postnatal rat brain extract; no marked differences in expression of NR3B were found for either age. Conclusions. This is the first research using native protein for recognition of the NR3 subunit of the NMDA receptor It shows the antibody specificity and contributes to understanding the receptor's functions and its relation to spatial memory regulation. [ABSTRACT FROM AUTHOR]

Based on the analgesic effect of NMDA antagonist receptors, the nociceptive action of the peptide BLMP-101 is evaluated, agonist of NMDA, designed to boost learning/memory. 32 Wistar rats (male and female) were divided into four groups and were injected IP with different BLMP-101 doses (0.01 mg, 0.1 mg, and 0.5 mg) and a control group with physiological saline solution, during 11 days. Daily behavior of animals was registered 15 minutes after injection, and appearance of 26 nociceptive related variables was checked. Data was analyzed by mixed variance with α < 0.05. No important alterations were found. Results suggest that the BLMP-101 peptide does not present nociceptive activity at levels and periodicity used in this study. [ABSTRACT FROM AUTHOR]