LEAping to conclusions: a computational reanalysis of late embryogenesis abundant proteins and their possible roles.

RIGHTS : This article is licensed under the BioMed Central licence at http://www.biomedcentral.com/about/license which is similar to the 'Creative Commons Attribution Licence'. In brief you may : copy, distribute, and display the work; make derivative works; or make commercial use of the work - under the following conditions: the original author must be given credit; for any reuse or distribution, it must be made clear to others what the license terms of this work are.BACKGROUND: The late embryogenesis abundant (LEA) proteins cover a number of loosely related groups of proteins, originally found in plants but now being found in non-plant species. Their precise function is unknown, though considerable evidence suggests that LEA proteins are involved in desiccation resistance. Using a number of statistically-based bioinformatics tools the classification of a large set of LEA proteins, covering all Groups, is reexamined together with some previous findings. Searches based on peptide composition return proteins with similar composition to different LEA Groups; keyword clustering is then applied to reveal keywords and phrases suggestive of the Groups' properties. RESULTS: Previous research has suggested that glycine is characteristic of LEA proteins, but it is only highly over-represented in Groups 1 and 2, while alanine, thought characteristic of Group 2, is over-represented in Group 3, 4 and 6 but under-represented in Groups 1 and 2. However, for LEA Groups 1 2 and 3 it is shown that glutamine is very significantly over-represented, while cysteine, phenylalanine, isoleucine, leucine and tryptophan are significantly under-represented. There is also evidence that the Group 4 LEA proteins are more appropriately redistributed to Group 2 and Group 3. Similarly, Group 5 is better found among the Group 3 LEA proteins. CONCLUSIONS: There is evidence that Group 2 and Group 3 LEA proteins, though distinct, might be related. This relationship is also evident in the overlapping sets of keywords for the two Groups, emphasising alpha-helical structure and, at a larger scale, filaments, all of which fits well with experimental evidence that proteins from both Groups are natively unstructured, but become structured under stress conditions. The keywords support localisation of LEA proteins both in the nucleus and associated with the cytoskeleton, and a mode of action similar to chaperones, perhaps the cold shock chaperones, via a role in DNA-binding. In general, non-globular and low-complexity proteins, such as the LEA proteins, pose particular challenges in determining their functions and modes of action. Rather than masking off and ignoring low-complexity domains, novel tools and tool combinations are needed which are capable of analysing such proteins in their entirety

Court Disregards Legislative History of the Civil Rights Act of 1991 and Bucks Current Trends Regarding Punitive Damages

Kolstad v. American Dental Ass\u27n, 108 F.3d 1431 (D.C. Cir. 1996)

Minimal Extension of the Standard Model Scalar Sector

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Welcome to Microbial Informatics and Experimentation

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How Magnetic is the Dirac Neutrino?

We derive model-independent, "naturalness" upper bounds on the magnetic moments \mu_\nu of Dirac neutrinos generated by physics above the scale of electroweak symmetry breaking. In the absence of fine-tuning of effective operator coefficients, we find that current information on neutrino mass implies that |\mu_\nu | < 10^(-14) Bohr magnetons. This bound is several orders of magnitude stronger than those obtained from analyses of solar and reactor neutrino data and astrophysical observations.Comment: 4 pages, 3 figures, Majorana case discussion corrected. References updated; replaced to match published versio

Towards a High Energy Theory for the Higgs Phase of Gravity

Spontaneous Lorentz violation due to a time-dependent expectation value for a massless scalar has been suggested as a method for dynamically generating dark energy. A natural candidate for the scalar is a Goldstone boson arising from the spontaneous breaking of a U(1) symmetry. We investigate the low-energy effective action for such a Goldstone boson in a general class of models involving only scalars, proving that if the scalars have standard kinetic terms then at the {\em classical} level the effective action does not have the required features for spontaneous Lorentz violation to occur asymptotically $(t \to \infty)$ in an expanding FRW universe. Then we study the large $N$ limit of a renormalizable field theory with a complex scalar coupled to massive fermions. In this model an effective action for the Goldstone boson with the properties required for spontaneous Lorentz violation can be generated. Although the model has shortcomings, we feel it represents progress towards finding a high energy completion for the Higgs phase of gravity.Comment: 20 pages, 5 figures;fixed typos and added reference

Resistant Somatoform Symptoms: Try CBT and Antidepressants. Preferred Strategy for ‘Mismatched’ Category of Illnesses.

This articles describes: debate about how to categorize somatoform disorders--as psychological or physiologic evidence supporting psychotherapy and antidepressants to help patients with treatment-resistant somatoform disorders

Heavy Quark Fragmentation to Baryons Containing Two Heavy Quarks

We discuss the fragmentation of a heavy quark to a baryon containing two heavy quarks of mass $m_Q\gg\Lambda_{\rm QCD}$. In this limit the heavy quarks first combine perturbatively into a compact diquark with a radius small compared to $1/\Lambda_{\rm QCD}$, which interacts with the light hadronic degrees of freedom exactly as does a heavy antiquark. The subsequent evolution of this $QQ$ diquark to a $QQq$ baryon is identical to the fragmentation of a heavy antiquark to a meson. We apply this analysis to the production of baryons of the form $ccq$, $bbq$, and $bcq$.Comment: 9 pages, 1 figure included, uses harvmac.tex and epsf.tex, UCSD/PTH 93-11, CALT-68-1868, SLAC-PUB-622