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List of Antarctic expeditions

This list of Antarctic expeditions is a chronological list of expeditions involving Antarctica. Although the existence of a southern continent had been hypothesized as early as the writings of Ptolemy in the 1st century AD, the South Pole was not reached until 1911. 600 BC – 300 BC – Greek Philosophers theorize Spherical Earth with North and South Polar regions. 150 AD – Ptolemy published Geographia, which notes Terra Australis Incognita. 7th century – Ui-te-Rangiora claimed to have sighted southern ice fields. 13th century – Polynesians settle Auckland Islands 1501–1502 – Gonçalo Coelho and Amerigo Vespucci sail to 1522 – Ferdinand Magellan – first circumnavigation discovers Strait of Magellan 1578 – Francis Drake claims to have discovered an ocean south of South America and "Elizabeth Island" 1599 – Dirk Gerritsz – sails to 1603 – Gabriel de Castilla – sails to 1615 – Jacob le Maire and Willem Schouten first to sail around Cape Horn cross 1619 – Garcia de Nodal expedition – circumnavigate Tierra del Fuego and discover Diego Ramírez Islands 1643 – Dutch expedition to Valdivia – northerly winds push the expedition as far south as 61°59 S where icebergs were abundant.

The expedition disproves beliefs. 1675 – Anthony de la Roché discovers South Georgia, the first land discovered south of the Antarctic Convergence 1698–1699 – Edmond Halley sails to 1720 – Captain George Shelvocke – sails to 1739 – Jean-Baptiste Charles Bouvet de Lozier – discovers Bouvet Island 1771 – James CookHM Bark Endeavour expedition 1771–1772 – First French Antarctic Expedition – led by Yves-Joseph de Kerguelen-Trémarec discovers Kerguelen Islands 1772–1775 – James Cook – sails HMS Resolution crossing Antarctic Circle in January 1773 and December 1773. On 30 January 1774 he reaches 71° 10′ S, his Farthest South, coming within about 75 miles of the Antarctic mainland without seeing it. 1780s to 1839 – American and British whalers and sealers make incidental discoveries. 1819 – William Smith discovers South Shetland Islands, the first land discovered south of 60° south latitude. 1819 – San Telmo wrecks in the Drake Passage off Livingston Island. 1819–1821 – Fabian Gottlieb von Bellingshausen and Mikhail Lazarev, Admirals of Russian Imperial Navy, during Russian circumnavigation expedition, on 27 January 1820, discovers an ice shelf at Princess Martha Coast that became known as the Fimbul Ice Shelf.

Bellingshausen and Lazarev became the first explorers to see and discover the land of Antarctica. 1820 – Edward Bransfield with William Smith as his pilot – on 30 January 1820, sight Trinity Peninsula. 1820 – Nathaniel Palmer sights Antarctica on 17 November 1820 1821 – George Powell, a British sealer, Nathaniel B. Palmer, an American sealer, discover the South Orkney Islands. Powell annexes them for the British. 1821 – John Davis – on 7 February 1821 disputed claim of setting foot on Antarctica at Hughes Bay 1823–1824 – James Weddell discovers the Weddell Sea. 1872–1876 – HMS Challenger under Capt. George S. Nares, becomes the first steamship to cross the Antarctic Circle. 1892–1893 – Carl Anton Larsen led the first Norwegian expedition to Antarctica aboard the ship Jason. Larsen became the first person to ski in Antarctica. 1892–1893 – Dundee Whaling Expedition discover Dundee Island 1893–1894 – Carl Anton Larsen led the second Norwegian expedition to Antarctica 1893–1895 – Henryk Bull, Carstens Borchgrevink and Alexander von Tunzelmann – set foot on Antarctica at Cape Adare 1897–1899 – Belgian Antarctic Expedition – led by Adrien de Gerlache.

Boxcar Bertha

Boxcar Bertha is a low budget 1972 American romantic crime drama film directed by Martin Scorsese. It is a loose adaptation of Sister of the Road, a pseudo-autobiographical account of the fictional character Bertha Thompson, written by Ben L. Reitman, it was Scorsese's second feature film. The film tells the story of Boxcar Bertha Thompson and "Big" Bill Shelly, two train robbers and lovers who are caught up in the plight of railroad workers in the American South; when Bertha is implicated in the murder of a wealthy gambler, the pair become fugitives. Barbara Hershey as Boxcar Bertha David Carradine as Big Bill Shelly Barry Primus as Rake Brown Bernie Casey as Von Morton John Carradine as H. Buckram Sartoris Harry Northup as Harvey Hall Victor Argo as First McIver After the success of Bloody Mama, Roger Corman wanted to make another female gangster film. Julie Corman came across the story of Boxcar Bertha. Martin Scorsese was hired to direct on the strength of his first feature, he was given the lead actors, including Barbara Hershey, David Carradine, Barry Primus, a shooting schedule of 24 days in Arkansas.

The Reader Railroad was used for the train scenes. The locomotive in those scenes was 1920 Baldwin 2-6-2 #108, who saw service on the Conway Scenic Railroad in the late 1970s; the engine is at the Blacklands Railroad yard in Sulphur Springs Texas, awaiting restoration. Locomotive #1702, a USATC S160 2-8-0 built by Baldwin in 1942, was seen in the film as well; the locomotive is now operational at the Great Smoky Mountains Railroad. Scorsese makes a cameo in the film as one of Bertha's clients during the brothel montage. Hershey called the film "a lot of fun though it's crippled by Roger Corman and the violence and sex, but between the actors and Marty Scorsese the director, we had a lot of fun. We had characters down but one tends to not see all that, because you end up seeing all the blood and sex." Boxcar Bertha received mixed reviews from critics. It holds a rating of 52% on Rotten Tomatoes based on 23 reviews. Roger Ebert of the Chicago Sun-Times gave the film 3 stars out of 4 and called it "a weirdly interesting movie...

Director Martin Scorsese has gone for mood and atmosphere more than for action, his violence is always blunt and unpleasant — never liberating and exhilarating, as the New Violence is supposed to be. We get the feeling we're inhabiting the dark night of a soul." Howard Thompson of The New York Times found the film an "interesting surprise," with an "excellent" performance by Carradine and "beautiful" direction by Scorsese, "who comes into his own here." Arthur D. Murphy of Variety was negative, writing, "Whatever its intentions,'Boxcar Bertha' is not much more than an excuse to slaughter a lot of people... The final cut has stripped away whatever mood and motivation may have been in the script, leaving little more than fights, shotgun blasts and aimless movement." Gene Siskel of the Chicago Tribune gave the film 1 star out of 4 and called it a "trashy movie" with violence that "does not shock. It depresses." Kevin Thomas of the Los Angeles Times wrote, "What is most impressive about'Boxcar Bertha'... is how 28-year old director Martin Scorsese, in his first Hollywood venture, has managed to shape such familiar material into a viable film."

Tom Milne of The Monthly Film Bulletin declared: "Abrasively scripted, stunningly shot, beautifully acted by David Carradine, Barbara Hershey and Barry Primus in particular, Boxcar Bertha is much more than the exploitation picture it has been written off as and makes a worthy companion piece to both Bloody Mama and Bonnie and Clyde." List of American films of 1972 Boxcar Bertha on IMDb Boxcar Bertha at AllMovie Boxcar Bertha at the TCM Movie Database Boxcar Bertha at Rotten Tomatoes

Hydrophobin

Hydrophobins are a group of small cysteine-rich proteins that are expressed only filamentous fungi and lichens. They are known for their ability to form a hydrophobic coating on the surface of an object, they were first discovered and separated in Schizophyllum commune in 1991. Based on differences in hydropathy patterns and biophysical properties, they can be divided into two categories: class I and class II. Hydrophobins can self-assemble into a monolayer on hydrophilic:hydrophobic interfaces such as a water:air interface. Class I monolayer contains the same core structure as amyloid fibrils, is positive to Congo red and thioflavin T; the monolayer formed by class I hydrophobins has a ordered structure, can only be dissociated by concentrated trifluoroacetate or formic acid. Monolayer assembly involves large structural rearrangements with respect to the monomer. Fungi make complex aerial structures and spores in aqueous environments. Hydrophobins have been identified in lichens and basidiomycetes.

Hydrophobins are found on the outer surface of conidia and of the hyphal wall, may be involved in mediating contact and communication between the fungus and its environment. Some family members contain multiple copies of the domain. Hydrophobins have been found to be structurally and functionally similar to cerato-platanins, another group of small cysteine-rich proteins, which contain a high percentage of hydrophobic amino acids, are associated with hyphal growth; this family of proteins includes the rodlet proteins of Neurospora crassa and Emericella nidulans, these proteins are the main component of the hydrophobic sheath covering the surface of many fungal spores. Genomic sequencing of two fungi from dry or salty environments revealed that these species contain predicted hydrophobins with unusually high proportion of acidic amino acids and therefore with novel characteristics. High proportion of acidic amino acids is thought to be an adaptation of proteins to high concentrations of salt.

Hydrophobins are characterised by the presence of 8 conserved cysteine residues that form 4 disulphide bonds. They are able to reverse the wettability of surfaces by spontaneous self-assembly of the monomeric proteins into amphipathic monolayers at hydrophobic:hydrophilic surfaces. Despite this common feature, hydrophobins are subdivided into two classes based on differences on their monomeric structure, such as the spacing between the cysteine residues, based on the different physicochemical properties of the amphipathic monolayers they form. Extensive structural analyses of individual hydrophobins from the two classes have elucidated that the morphological and physical differences between the class I and class II polymer forms are the results of significant structural differences at the monomer-assembly level. Class I hydrophobins are characterised by having a quite diverse amino acid sequence between different types, compared to class II, they have long, varied inter-cysteine spacing, they form rodlets which have been identified as functional amyloids due to their amyloid-like characteristics as seen in X-ray diffraction studies and confirmed by their capacity to bind to amyloid-specific dyes such as Congo red and Thioflavin T.

The formation of rodlets involves conformational changes that lead to formation of an robust β-sheet structure that can only be depolymerised by treatment with strong acids. The rodlets can spontaneously form ordered monolayers by lateral assembly, displaying a regular fibrillary morphology on hydrophobic:hydrophilic interfaces; the most well characterised class I hydrophobin is EAS, which coats the spores of the fungus Neurospora crassa, followed by characterisation of DewA from Aspergillus nidulans. Class II hydrophobins have overall a more conserved amino acid sequence between the different types and, contrary to class, I they have short, regular inter-cysteine spacing. Opposite to class I, the class II hydrophobins monolayer formed at hydrophobic:hydrophilic interfaces is not fibrillar and it is not associated with formation of amyloid-structures, nor with large conformational changes. Nonetheless, high resolution atomic-force microscopy studies revealed the formation of a notable hexagonal repeating pattern over surfaces coated with the class II hydrophobin HBFI, meaning that these proteins are able to form an ordered network in surface films.

The crystal structures or HFBI and HFBII from Trichoderma reesei were the first class II hydrophobins to be determined. There is special interest in understanding the mechanism underlying class I monomers self-assembly that leads to formation of tough, ordered amphipathic rodlet monolayers, due to their intrinsic properties and due to substantial information available from several characterisation studies of the class I hydrophobins EAS and DewA; these mechanisms have been studied by targeted mutagenesis in an effort to identify the key amino acid sequence regions driving rodlet self-assembly. A model for the monomeric form of EAS was proposed by Kwan et al. from structural data obtained from NMR spectroscopy and X-ray diffraction experiments that indicated the presence of four-stranded, antiparallel β-barrel core structure in EAS that allows monomer linking through backbone H-bonding. There are secondary elements around this β-barrel core like the Cys7-Cys8 loops; this model is consistent with the amyloid-like structure that class I rodlets form, in which the β-strands are oriented perpendicular to the cross-β scaffold axis of the fibre.

Site-directed mutagenesis of EAS has given insights into the specific structural chang