On the Emergent Spectra of Hot Protoplanet Collision Afterglows

We explore the appearance of terrestrial planets in formation by studying the emergent spectra of hot molten protoplanets during their collisional formation. While such collisions are rare, the surfaces of these bodies may remain hot at temperatures of 1000-3000 K for up to millions of years during the epoch of their formation. These object are luminous enough in the thermal infrared to be observable with current and next generation optical/IR telescopes, provided that the atmosphere of the forming planet permits astronomers to observe brightness temperatures approaching that of the molten surface. Detectability of a collisional afterglow depends on properties of the planet's atmosphere -- primarily on the mass of the atmosphere. A planet with a thin atmosphere is more readily detected, because there is little atmosphere to obscure the hot surface. Paradoxically, a more massive atmosphere prevents one from easily seeing the hot surface, but also keeps the planet hot for a longer time. In terms of planetary mass, more massive planets are also easier to detect than smaller ones because of their larger emitting surface areas. We present preliminary calculations assuming a range of protoplanet masses (1-10 M_\earth), surface pressures (1-1000 bar), and atmospheric compositions, for molten planets with surface temperatures ranging from 1000 to 1800 K, in order to explore the diversity of emergent spectra that are detectable. While current 8- to 10-m class ground-based telescopes may detect hot protoplanets at wide orbital separations beyond 30 AU (if they exist), we will likely have to wait for next-generation extremely large telescopes or improved diffraction suppression techniques to find terrestrial planets in formation within several AU of their host stars.Comment: 28 pages, 6 figures, ApJ manuscript format, accepted into the Ap

Is Gliese 581d habitable? Some constraints from radiative-convective climate modeling

The recently discovered exoplanet Gl581d is extremely close to the outer edge of its system's habitable zone, which has led to much speculation on its possible climate. We have performed a range of simulations to assess whether, given simple combinations of chemically stable greenhouse gases, the planet could sustain liquid water on its surface. For best estimates of the surface gravity, surface albedo and cloud coverage, we find that less than 10 bars of CO2 is sufficient to maintain a global mean temperature above the melting point of water. Furthermore, even with the most conservative choices of these parameters, we calculate temperatures above the water melting point for CO2 partial pressures greater than about 40 bar. However, we note that as Gl581d is probably in a tidally resonant orbit, further simulations in 3D are required to test whether such atmospheric conditions are stable against the collapse of CO2 on the surface.Comment: 9 pages, 11 figures. Accepted for publication in Astronomy & Astrophysic

Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein.

Bacteria exploit surface proteins to adhere to other bacteria, surfaces and host cells. Such proteins need to project away from the bacterial surface and resist significant mechanical forces. SasG is a protein that forms extended fibrils on the surface of Staphylococcus aureus and promotes host adherence and biofilm formation. Here we show that although monomeric and lacking covalent cross-links, SasG maintains a highly extended conformation in solution. This extension is mediated through obligate folding cooperativity of the intrinsically disordered E domains that couple non-adjacent G5 domains thermodynamically, forming interfaces that are more stable than the domains themselves. Thus, counterintuitively, the elongation of the protein appears to be dependent on the inherent instability of its domains. The remarkable mechanical strength of SasG arises from tandemly arrayed 'clamp' motifs within the folded domains. Our findings reveal an elegant minimal solution for the assembly of monomeric mechano-resistant tethers of variable length.This research was supported by Biotechnology and Biological Research Council Grants BB/J006459/1 (D.T.G. and J.C.), BB/J005029/1 (F.W. and J.R.P), BB/G019452/1 (O.E.F and D.J.B) and BB/G020671/1 (C.G.B. and J.R.P.). H.K.H.F. is supported by a studentship from a Wellcome Trust 4-year PhD programme (WT095024MA). C.M.J. is supported by the German Federal Ministry of Education and Research (BMBF), grant BIOSCAT (contract N° 05K12YE1). J.C. is a Wellcome Trust Senior Research Fellow (WT/095195). J.R.P holds a British Heart Foundation Senior Basic Science Fellowship (FS/12/36/29588). The authors acknowledge the use of EMBL SAXS beamline P12 at Petra-3 (DESY, Hamburg, Germany) and Maxim Petoukhov (EMBL) for providing a modified version of SASR EF. The research leading to these results has received funding from the European Community's Seventh Framework Programme (FP7/2007-2013) under BioStruct-X (grant agreement N°283570). The authors would like to thank Diamond Light Source for beamtime (proposal mx-7864) and Johan Turkenburg and Sam Hart for assistance with crystal testing and data collection.This is the final version of the article. It first appeared from NPG via http://dx.doi.org/10.1038/ncomms827

Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein

Bacteria exploit surface proteins to adhere to other bacteria, surfaces and host cells. Such proteins need to project away from the bacterial surface and resist significant mechanical forces. SasG is a protein that forms extended fibrils on the surface of Staphylococcus aureus and promotes host adherence and biofilm formation. Here we show that although monomeric and lacking covalent cross-links, SasG maintains a highly extended conformation in solution. This extension is mediated through obligate folding cooperativity of the intrinsically disordered E domains that couple non-adjacent G5 domains thermodynamically, forming interfaces that are more stable than the domains themselves. Thus, counterintuitively, the elongation of the protein appears to be dependent on the inherent instability of its domains. The remarkable mechanical strength of SasG arises from tandemly arrayed 'clamp' motifs within the folded domains. Our findings reveal an elegant minimal solution for the assembly of monomeric mechano-resistant tethers of variable length

Disorder drives cooperative folding in a multidomain protein.

Many human proteins contain intrinsically disordered regions, and disorder in these proteins can be fundamental to their function-for example, facilitating transient but specific binding, promoting allostery, or allowing efficient posttranslational modification. SasG, a multidomain protein implicated in host colonization and biofilm formation in Staphylococcus aureus, provides another example of how disorder can play an important role. Approximately one-half of the domains in the extracellular repetitive region of SasG are intrinsically unfolded in isolation, but these E domains fold in the context of their neighboring folded G5 domains. We have previously shown that the intrinsic disorder of the E domains mediates long-range cooperativity between nonneighboring G5 domains, allowing SasG to form a long, rod-like, mechanically strong structure. Here, we show that the disorder of the E domains coupled with the remarkable stability of the interdomain interface result in cooperative folding kinetics across long distances. Formation of a small structural nucleus at one end of the molecule results in rapid structure formation over a distance of 10 nm, which is likely to be important for the maintenance of the structural integrity of SasG. Moreover, if this normal folding nucleus is disrupted by mutation, the interdomain interface is sufficiently stable to drive the folding of adjacent E and G5 domains along a parallel folding pathway, thus maintaining cooperative folding.This research was supported by Biotechnology and Biological Research Council Grants BB/J006459/1 (D.T.G. and J.C.), BB/J005029/1 (F.W. and J.R.P), C.A.T.F.M is supported by the Cambridge Trust and CAPES Science without Borders Cambridge Scholarship. J.R.P holds a British Heart Foundation Senior Basic Science Fellowship (FS/12/36/29588). J.C. is a Wellcome Trust Senior Research Fellow (WT/095195)

Global modelling of the early Martian climate under a denser CO2 atmosphere: Water cycle and ice evolution

We discuss 3D global simulations of the early Martian climate that we have performed assuming a faint young Sun and denser CO2 atmosphere. We include a self-consistent representation of the water cycle, with atmosphere-surface interactions, atmospheric transport, and the radiative effects of CO2 and H2O gas and clouds taken into account. We find that for atmospheric pressures greater than a fraction of a bar, the adiabatic cooling effect causes temperatures in the southern highland valley network regions to fall significantly below the global average. Long-term climate evolution simulations indicate that in these circumstances, water ice is transported to the highlands from low-lying regions for a wide range of orbital obliquities, regardless of the extent of the Tharsis bulge. In addition, an extended water ice cap forms on the southern pole, approximately corresponding to the location of the Noachian/Hesperian era Dorsa Argentea Formation. Even for a multiple-bar CO2 atmosphere, conditions are too cold to allow long-term surface liquid water. Limited melting occurs on warm summer days in some locations, but only for surface albedo and thermal inertia conditions that may be unrealistic for water ice. Nonetheless, meteorite impacts and volcanism could potentially cause intense episodic melting under such conditions. Because ice migration to higher altitudes is a robust mechanism for recharging highland water sources after such events, we suggest that this globally sub-zero, `icy highlands' scenario for the late Noachian climate may be sufficient to explain most of the fluvial geology without the need to invoke additional long-term warming mechanisms or an early warm, wet Mars.Comment: Minor revisions to text, one new table, figs. 1,3 11 and 18 redon

Visualization of direct and diffusion-assisted RAD51 nucleation by full-length human BRCA2 protein

Homologous recombination (HR) is essential for error-free repair of DNA double-strand breaks, perturbed replication forks (RFs), and post-replicative single-stranded DNA (ssDNA) gaps. To initiate HR, the recombination mediator and tumor suppressor protein BRCA2 facilitates nucleation of RAD51 on ssDNA prior to stimulation of RAD51 filament growth by RAD51 paralogs. Although ssDNA binding by BRCA2 has been implicated in RAD51 nucleation, the function of double-stranded DNA (dsDNA) binding by BRCA2 remains unclear. Here, we exploit single-molecule (SM) imaging to visualize BRCA2-mediated RAD51 nucleation in real time using purified proteins. We report that BRCA2 nucleates and stabilizes RAD51 on ssDNA either directly or through an unappreciated diffusion-assisted delivery mechanism involving binding to and sliding along dsDNA, which requires the cooperative action of multiple dsDNA-binding modules in BRCA2. Collectively, our work reveals two distinct mechanisms of BRCA2-dependent RAD51 loading onto ssDNA, which we propose are critical for its diverse functions in maintaining genome stability and cancer suppression