SUMMARY / RELATED TOPICS

Topographic map

In modern mapping, a topographic map or topographic chart is a type of map characterized by large-scale detail and quantitative representation of relief using contour lines, but using a variety of methods. Traditional definitions require a topographic map to show both man-made features. A topographic survey is published as a map series, made up of two or more map sheets that combine to form the whole map. A contour line is a line connecting places of equal elevation. Natural Resources Canada provides this description of topographic maps:These maps depict in detail ground relief, forest cover, administrative areas, populated areas, transportation routes and facilities, other man-made features. Other authors define topographic maps by contrasting them with another type of map. However, in the vernacular and day to day world, the representation of relief is popularly held to define the genre, such that small-scale maps showing relief are called "topographic"; the study or discipline of topography is a much broader field of study, which takes into account all natural and man-made features of terrain.

Topographic maps are based on topographical surveys. Performed at large scales, these surveys are called topographical in the old sense of topography, showing a variety of elevations and landforms; this is in contrast to older cadastral surveys, which show property and governmental boundaries. The first multi-sheet topographic map series of an entire country, the Carte géométrique de la France, was completed in 1789; the Great Trigonometric Survey of India, started by the East India Company in 1802 taken over by the British Raj after 1857 was notable as a successful effort on a larger scale and for determining heights of Himalayan peaks from viewpoints over one hundred miles distant. Topographic surveys were prepared by the military to assist in planning for battle and for defensive emplacements; as such, elevation information was of vital importance. As they evolved, topographic map series became a national resource in modern nations in planning infrastructure and resource exploitation. In the United States, the national map-making function, shared by both the Army Corps of Engineers and the Department of the Interior migrated to the newly created United States Geological Survey in 1879, where it has remained since.1913 saw the beginning of the International Map of the World initiative, which set out to map all of Earth's significant land areas at a scale of 1:1 million, on about one thousand sheets, each covering four degrees latitude by six or more degrees longitude.

Excluding borders, each sheet was up to 66 cm wide. Although the project foundered, it left an indexing system that remains in use. By the 1980s, centralized printing of standardized topographic maps began to be superseded by databases of coordinates that could be used on computers by moderately skilled end users to view or print maps with arbitrary contents and scale. For example, the Federal government of the United States' TIGER initiative compiled interlinked databases of federal and local political borders and census enumeration areas, of roadways and water features with support for locating street addresses within street segments. TIGER was used in the 1990 and subsequent decennial censuses. Digital elevation models were compiled from topographic maps and stereographic interpretation of aerial photographs and from satellite photography and radar data. Since all these were government projects funded with taxes and not classified for national security reasons, the datasets were in the public domain and usable without fees or licensing.

TIGER and DEM datasets facilitated Geographic information systems and made the Global Positioning System much more useful by providing context around locations given by the technology as coordinates. Initial applications were professionalized forms such as innovative surveying instruments and agency-level GIS systems tended by experts. By the mid-1990s user-friendly resources such as online mapping in two and three dimensions, integration of GPS with mobile phones and automotive navigation systems appeared; as of 2011, the future of standardized, centrally printed topographical maps is left somewhat in doubt. Topographic maps have multiple uses in the present day: any type of geographic planning or large-scale architecture; the various features shown on the map are represented by conventional symbols. For example, colors can be used to indicate a classification of roads; these signs are explained in the margin of the map, or on a separately published characteristic sheet. Topographic maps are commonly called contour maps or topo maps.

In the United States, where the primary national series is organized by a strict 7.5-minute grid, they are called topo quads or quadrangles. Topographic maps conventionally show land contours, by means of contour lines. Contour lines are curves. In other words, every point on the marked line of 100 m elevation is 100 m above mean sea level. Th

Protein tertiary structure

Protein tertiary structure is the three dimensional shape of a protein. The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains may bond in a number of ways; the interactions and bonds of side chains within a particular protein determine its tertiary structure. The protein tertiary structure is defined by its atomic coordinates; these coordinates may refer either to the entire tertiary structure. A number of tertiary structures may fold into a quaternary structure; the science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition. Although Emil Fischer had suggested proteins were made of polypeptide chains and amino acid side chains, it was Dorothy Maud Wrinch who incorporated geometry into the prediction of protein structures. Wrinch demonstrated this with the Cyclol model, the first prediction of the structure of a globular protein. Contemporary methods are able to determine, without prediction, tertiary structures to within 5 Å for small proteins and, under favorable conditions, confident secondary structure predictions.

A protein folded into its native state or native conformation has a lower Gibbs free energy than the unfolded conformation. A protein will tend towards low-energy conformations, which will determine the protein's fold in the cellular environment; because many similar conformations will have similar energies, protein structures are dynamic, fluctuating between a large these similar structures. Globular proteins have a core of hydrophobic amino acid residues and a surface region of water-exposed, hydrophilic residues; this arrangement may stabilise interactions within the tertiary structure. For example, in secreted proteins, which are not bathed in cytoplasm, disulfide bonds between cysteine residues help to maintain the tertiary structure. There is a commonality of stable tertiary structures seen in proteins of diverse function and diverse evolution. For example, the TIM barrel, named for the enzyme triosephosphateisomerase, is a common tertiary structure as is the stable, coiled coil structure.

Hence, proteins may be classified by the structures. Databases of proteins which use such a classification include SCOP and CATH. Folding kinetics may trap a protein in a high-energy conformation, i.e. a high-energy intermediate conformation blocks access to the lowest-energy conformation. The high-energy conformation may contribute to the function of the protein. For example, the influenza hemagglutinin protein is a single polypeptide chain which when activated, is proteolytically cleaved to form two polypeptide chains; the two chains are held in a high-energy conformation. When the local pH drops, the protein undergoes an energetically favorable conformational rearrangement that enables it to penetrate the host cell membrane; some tertiary protein structures may exist in long-lived states that are not the expected most stable state. For example, many serpins show this metastability, they undergo a conformational change. It is assumed that the native state of a protein is the most thermodynamically stable and that a protein will reach its native state, given its chemical kinetics, before it is translated.

Protein chaperones within the cytoplasm of a cell assist a newly synthesised polypeptide to attain its native state. Some chaperone proteins are specific in their function, for example, protein disulfide isomerase. Prediction of protein tertiary structure relies on knowing the protein's primary structure and comparing the possible predicted tertiary structure with known tertiary structures in protein data banks; this only takes into account the cytoplasmic environment present at the time of protein synthesis to the extent that a similar cytoplasmic environment may have influenced the structure of the proteins recorded in the protein data bank. The structure of a protein, for example an enzyme, may change upon binding of its natural ligands, for example a cofactor. In this case, the structure of the protein bound to the ligand is known as holo structure, of the unbound protein as apo structure; the knowledge of the tertiary structure of soluble globular proteins is more advanced than that of membrane proteins because the former are easier to study with available technology.

X-ray crystallography is the most common tool used to determine protein structure. It provides high resolution of the structure but it does not give information about protein's conformational flexibility. Protein NMR gives comparatively lower resolution of protein structure, it is limited to smaller proteins. However, it can provide information about conformational changes of a protein in solution. Cryogenic electron microscopy can give information about both a protein's tertiary and quaternary structure, it is well-suited to large proteins and symetrical complexes of protein subunits. Dual polarisation interferometry provides complementary information about surface captured proteins, it assists in determining conformation changes over time. The Folding@home project at Stanford University is a distributed computing research effort which uses 5 petaFLOPS of available computing, it aims to find an algorithm which will predict protein tertiary and quaternary structures given the protein's amino acid sequence and its

Buntingsdale Hall

Buntingsdale Hall is a historic country house in the parish of Sutton upon Tern, to the southwest of Market Drayton in Shropshire, England. It became a Grade II* listed building on 14 February 1979. Buntingsdale Hall was first built for Bulkeley Mackworth and the Mackworth family between 1719 and 1721; the plans for the building were drawn up by the London architect and surveyor John Prince, although it was completed by Francis Smith of Warwick. Documents have revealed that Mackworth may have encountered a dispute with Prince and dismissed him and hired Francis Smith to complete the building; the estate included the remains of Fordhall castle, a monument scheduled under the Ancient Monuments and Archaeological Areas Act 1979 Herbert Mackworth sold the hall to his cousin William Tayleur, who subsequently owned the property for many years. He gives his name to the road that leads to the hall. In 1986, during the time that a survey was conducted of the property, it was reported that a number of furnishings had been stolen from the hall.

By 2000 the hall was placed on the Historic Buildings at Risk register. Subsequently it was renovated and was removed from this register in 2004. Over the years the hall has been owned by many different families but the current owners are Mackworths, direct descendants of Bulkeley Mackworth; the house is dated "1721" on the lead downpipe straps. It was extended and altered by Samuel Pountney Smith of Shrewsbury in 1857, it is a three-storey red brick building with red sandstone ashlar dressings, featuring some fluted pilasters and a Corinthian stone doorcase consisting of pilasters, each supporting a section of entablature. The rainwater heads are emblazoned with the Mackworth arms and crest, an acanthus ornament at the junction of pipes and cornice, straps have the initials "BM" and the date "1721"; the north wing is dated to 1857, with identical east and west fronts, when the staircase was moved and the full-height entrance hall was created. The entrance hallway has black and white stone flooring and bolection-moulded panelling up to first floor level with cornice.

The first-floor gallery above with turned balusters is raised to centre, the central first-floor doorway is made up of fluted pilasters and an open triangular pediment. It features a stone fireplace with cable-fluted Ionic columns; the dining room features a rich cornice with vine trail and egg and dart enrichment, added in 1857, when the fireplace was removed. The ballroom features the same style as the dining room, with rich plaster panelling. A garden was laid out with the house, covering an area of 16 hectares; the River Tern passes to the north of Buntingsdale Hall, with the main garden retaining wall west of the house, an apsidal bow overlooking the pond. The grounds were altered several times during the 18th and 19th centuries and walled gardens, a kitchen garden, large fishpond and boathouse, woodland were added. By the end of the 19th century, a new entrance from the north and a lodge had been added. Grade II* listed buildings in Shropshire Council Listed buildings in Sutton upon Tern