A revista Nature Chemical Biology não consta do portal CAPES/Periódicos por quê?

segunda-feira, novembro 09, 2009

Por que a revista Nature Chemical Biology não consta do portal CAPES/Periódicos? Será por que suas pesquisas em biologia química enfraquecem o gradualismo darwiniano e tornam robustas as teses de complexidade irredutível e informação complexa especificada da teoria do Design Inteligente???

Se for esta a razão, a decisão da CAPES está provocando um grande atraso da ciência no Brasil, e a sociedade brasileira precisa saber por que esta revista não consta da relação das publicações científicas (assinaturas) disponibilizadas naquele portal.

A CAPES com a palavra!

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In This Issue

Nature Chemical Biology 5, v (2009)

doi:10.1038/nchembio.254

In this issue

Focus on protein dynamics

At an elementary level, much can be learned about a protein's function from gazing at its sequence and determining its higher order structure. Beyond this, understanding their role in larger complexes and enzymatic reactions is critical to fully appreciate the machinery that is built from individual proteins. For example, proteins of the eukaryotic 26S proteasome, which is responsible for regulated degradation of a variety of proteins, must assemble into a complex that is sufficiently specific and discriminatory to avoid unwanted protein destruction. Proteins destined for degradation must contain several ubiquitin-modified residues as well as an unstructured region that acts as a degradation initiation site [Review, p. 815]. Such unstructured or "intrinsically disordered" and highly flexible protein (IDP) regions are common in eukaryotic proteins of diverse functions and call into question whether structure is inherently important for function. Tsvetkov et al. propose that IDPs have protective "nannies" that allow for proper maturation and formation of functional IDP-containing complexes [Commentary, p. 778]. Bound to a nanny, an IDP may obtain some level of folded functional structure that evokes the induced best-fit model for molecular recognition. As an alternative to this classic view, "conformational selection" predicts that ligands select the most favored conformation from a number of pre-existing conformations [Perspective, p. 789], some of which may be sparse and exist only transiently, and so are "invisible" to all but the most sophisticated NMR measurements [Review, p. 808]. Conformational variability is also the basis of flexible backbone design, which has recently emerged for engineering protein-protein interfaces [Review, p. 797]. Borrowing from the idea that the function of a protein is determined by the relationship between structure and dynamics, various optical techniques are available to monitor protein dynamics over a range of timescales not accessible by the more 'static' strategies of structural biology [Primer, insert]. Gierasch and Gershenson argue that improvements in techniques ranging from computational analysis of systems biology data to optical imaging should be taken as an invitation to embrace the post-reductionist era of biochemistry [Commentary, p. 774]. The fact that nearly every major cellular process is carried out by assemblies of ten or more proteins points to a need to work as often as possible in in vivo systems, or to develop new strategies when this is not possible. Monitoring protein dynamics is complementary to monitoring protein structure and is clearly contributing to a more full understanding of protein function, as outlined in the collection of pieces in this issue. MB