Affinity is a 1999 historical fiction novel by Sarah Waters. It is the author's second novel, following Tipping the Velvet, followed by Fingersmith. Margaret Prior, an unmarried woman from an upper-class family, visits the Millbank Prison in 1870s Victorian-era England; the protagonist is an overall unhappy person, recovering from her father's death and her subsequent suicide attempt, struggling with her lack of power living at home with her over-involved mother despite being 30. She becomes a "Lady Visitor" of the prison, hoping to escape her troubles and be a guiding figure in the lives of the female prisoners; as she peers through a flap in the door, entranced by the sight of a young woman with a flower, she is reminded of a Carlo Crivelli painting. Of all the prisoners, she is most fascinated by this woman, whom she learns to be Selina Dawes, medium of spirits. Arts Council of Wales Book of the Year Award, 2000 Ferro-Grumley Award for Lesbian and Gay Fiction, 2000 Lambda Literary Award for Fiction, 2000 Mail on Sunday/John Llewellyn Rhys Prize, 2000 Somerset Maugham Award, 2000 Sunday Times Young Writer of the Year Award, 2000 The novel was adapted into a screenplay by Andrew Davies.
A feature film based on Davies' adaptation of Affinity premiered on 19 June 2008 at the opening night of Frameline, the San Francisco International LGBT Film Festival, at the Castro Theater. The film was first shown on ITV1 in the United Kingdom on 28 December 2008
Affinity chromatography is a method of separating biochemical mixture based on a specific interaction between antigen and antibody and substrate, receptor and ligand, or protein and nucleic acid. It is a type of chromatographic laboratory technique used for purifying biological molecules within a mixture by exploiting molecular properties. Biological macromolecules, such as enzymes and other proteins, interact with other molecules with high specificity through several different types of bonds and interaction; such interactions include hydrogen bonding, ionic interaction, disulfide bridges, hydrophobic interaction, more. The high selectivity of affinity chromatography is caused by allowing the desired molecule to interact with the stationary phase and be bound within the column in order to be separated from the undesired material which will not interact and elute first; the molecules no longer needed are first washed away with a buffer while the desired proteins are let go in the presence of the eluting solvent.
This process creates a competitive interaction between the desired protein and the immobilized stationary molecules, which lets the now purified proteins be released. Affinity chromatography can be used to purify and concentrate a substance from a mixture into a buffering solution, reduce the amount of unwanted substances in a mixture, identify the biological compounds binding to a particular substance and concentrate an enzyme solution; the molecule of interest can be immobilized through covalent bonds. This occurs through an insoluble matrix such as chromatographic medium like cellulose or polyacrylamide; when the medium is bound to the protein of interest it becomes immobilized. Affinity chromatography is the basis for immunochromatographic test strips, which provide a rapid means of diagnosis in patient care. Using ICT, a technician can make a determination at a patient's bedside, without the need for a laboratory. ICT detection is specific to the microbe causing an infection. In summary, affinity chromatography exploits the differences in interactions' strengths between the different biomolecules within a mobile phase, the stationary phase.
The stationary phase is first loaded into a column with mobile phase containing a variety of biomolecules from DNA to proteins. The two phases are allowed time to bind. A wash buffer is poured through a column containing both bound phases; the wash buffer removes non-target biomolecules by disrupting their weaker interactions with the stationary phase. Target biomolecules have a much higher affinity for the stationary phase, remain bound to the stationary phase, not being washed away by wash buffer. An elution buffer is poured through the column containing the remaining target biomolecules; the elution buffer disrupts interactions between the bound target biomolecules with the stationary to a much greater extent than the wash buffer removing the target biomolecules. This purified solution contains elution buffer and target biomolecules, is called elution; the stationary phase is a gel matrix of agarose. To prevent steric interference or overlap during the binding process of the target molecule to the ligand, an inhibitor containing a hydrocarbon chain is first attached to the agarose bead.
This inhibitor with a hydrocarbon chain is known as the spacer between the agarose bead and the target molecule. The starting point is a crude, heterogeneous group of molecules in a whole cell extract, such as a cell lysate, growth medium or blood serum; the molecule of interest will have a well known and defined property, can be exploited during the affinity purification process. The process itself can be thought of as an entrapment, with the target molecule becoming trapped on a solid or stationary phase or medium; the other molecules in the mobile phase will not become trapped as they do not possess this property. The stationary phase can be removed from the mixture and the target molecule released from the entrapment in a process known as dialysis; the desired molecules are eluted with specific substances after washing the non-interacting molecules away. Thus, this results in a purified material. Specific elution of the desired macromolecule from the stationary phase is effected by adding to the eluting buffer a gradient of the same kind on the macromolecule and displaces it.
The most common use of affinity chromatography is for the purification of recombinant proteins. Affinity chromatography is an excellent choice for the first step in purifying a protein or nucleic acid from a crude mixture. If the molecular weight, charge, etc. of a protein is unknown, affinity chromatography can still apply to this situation. An example of this situation is when trying to find an enzyme with a particular activity, where it can be possible to build an affinity column with an attached ligand, similar or identical to the substrate of choice; the way that the desired enzyme would be eluted would be from the mixture based on the strong interaction of enzyme and the immobilized substrate analog, which would be done selectively through the affinity column. The elution of the enzyme with the appropriate substrate can be done. Binding to the solid phase may be achieved by column chromatography whereby the solid medium is packed onto a column, the initial mixture run through the column to allow settling, a wash buffer run through the column and the elution buffer subsequently applied to the column and collected.
These steps are done at ambient pressure. Alternatively, binding may be achieved using a batch treatment
Affinity electrophoresis is a general name for many analytical methods used in biochemistry and biotechnology. Both qualitative and quantitative information may be obtained through affinity electrophoresis; the methods include the so-called electrophoretic mobility shift assay, charge shift electrophoresis and affinity capillary electrophoresis. The methods are based on changes in the electrophoretic pattern of molecules through biospecific interaction or complex formation; the interaction or binding of a molecule, charged or uncharged, will change the electrophoretic properties of a molecule. Membrane proteins may be identified by a shift in mobility induced by a charged detergent. Nucleic acids or nucleic acid fragments may be characterized by their affinity to other molecules; the methods have been used for estimation of binding constants, as for instance in lectin affinity electrophoresis or characterization of molecules with specific features like glycan content or ligand binding. For enzymes and other ligand-binding proteins, one-dimensional electrophoresis similar to counter electrophoresis or to "rocket immunoelectrophoresis", affinity electrophoresis may be used as an alternative quantification of the protein.
Some of the methods are similar to affinity chromatography by use of immobilized ligands. There is ongoing research in developing new ways of utilizing the knowledge associated with affinity electrophoresis to improve its functionality and speed, as well as attempts to improve established methods and tailor them towards performing specific tasks. A type of electrophoretic mobility shift assay, agarose gel electrophoresis is used to separate protein-bound amino acid complexes from free amino acids. Using a low voltage to minimize the risk for heat damage, electricity is run across an agarose gel; this technique utilizes a high voltage with a 0.5× Tris-borate buffer run across an agarose gel. This method differs from the traditional agarose gel electrophoresis by utilizing a higher voltage to facilitate a shorter run time as well as yield a higher band resolution. Other factors included in developing the technique of rapid agarose gel electrophoresis are gel thickness, the percentage of agarose within the gel.
Boronate affinity electrophoresis utilizes boronic acid infused acrylimide gels to purify NAD-RNA. This purification allows for researchers to measure the kinetic activity of NAD-RNA decapping enzymes. Affinity capillary electrophoresis utilizes a formulary approach in accordance with the theory of electromigration; this method utilizes the inter-molecular interactions found in a free solution. "Affinity probes" consisting of fluorophore-labeled molecules that will bind to target molecules are mixed with the sample being tested. This mixture and its subsequent complexes are separated through capillary electrophoresis; the principle behind this type of electrophoresis is the mobility of the target molecules being altered by inter-molecular interactions. Affinity-trap polyacrylamide gel electrophoresis has become one of the most popular methods of protein separation; this is not only due to its separation qualities, but because it can be used in conjunction with a variety of other analytic methods, such as mass spectrometry, western blotting.
This method utilizes a two-step approach. First, a protein sample is run through a polyacrylamide gel using electrophoresis; the sample is transferred to a different polyacrylamide gel where affinity probes are immobilized. The proteins that do not have affinity for the affinity probes pass through the affinity-trap gel, proteins with affinity for the probes will be "trapped" by the immobile affinity probes; these trapped proteins are visualized and identified using mass spectrometry after in-gel digestion. Phosphate affinity electrophoresis utilizes an affinity probe which consists of a molecule that binds to divalent phosphate ions in neutral aqueous solution, known as a "Phos-Tag"; this methods utilizes a separation gel made of an acrylamide-pendent Phos-Tag monomer, copolymerized. Phosphorylated proteins migrate in the gel compared to non-phosphorylated proteins; this technique gives the researcher the ability to observe the differences in the phosphorylation states of any given protein. Immunoelectrophoresis Comprehensive texts edited by Niels H. Axelsen in Scandinavian Journal of Immunology, 1975 Volume 4 Supplement
In geometry, an affine transformation, affine map or an affinity is a function between affine spaces which preserves points, straight lines and planes. Sets of parallel lines remain parallel after an affine transformation. An affine transformation does not preserve angles between lines or distances between points, though it does preserve ratios of distances between points lying on a straight line. Examples of affine transformations include translation, homothety, similarity transformation, rotation, shear mapping, compositions of them in any combination and sequence. If X and Y are affine spaces every affine transformation f: X → Y is of the form x ↦ M x + b, where M is a linear transformation on the space X, x is a vector in X, b is a vector in Y. Unlike a purely linear transformation, an affine map need not preserve the zero point in a linear space. Thus, every linear transformation is affine. All Euclidean spaces are affine. In affine coordinates, which include Cartesian coordinates in Euclidean spaces, each output coordinate of an affine map is a linear function of all input coordinates.
Another way to deal with affine transformations systematically is to select a point as the origin. An affine map f: A → B between two affine spaces is a map on the points that acts linearly on the vectors. In symbols, f determines a linear transformation φ such that, for any pair of points P, Q ∈ A: f f → = φ or f − f = φ. We can interpret this definition in a few other ways. If an origin O ∈ A is chosen, B denotes its image f ∈ B this means that for any vector x →: f: ↦. If an origin O ′ ∈ B is chosen, this can be decomposed as an affine transformation g: A → B that sends O ↦ O ′, namely g: ↦,followed by the translation by a vector b → = O ′ B →; the conclusion is that, intuitively, f consists of a linear map. Given two affine spaces A and B, over the same field, a function f: A → B is an affine map if and only if for every family i ∈ I of weighted points in A such that ∑ i ∈ I λ i = 1,we have f = ∑ i ∈ I λ i f. I
In chemical physics and physical chemistry, chemical affinity is the electronic property by which dissimilar chemical species are capable of forming chemical compounds. Chemical affinity can refer to the tendency of an atom or compound to combine by chemical reaction with atoms or compounds of unlike composition; the idea of affinity is old. Many attempts have been made at identifying its origins; the majority of such attempts, except in a general manner, end in futility since "affinities" lie at the basis of all magic, thereby pre-dating science. Physical chemistry, was one of the first branches of science to study and formulate a "theory of affinity"; the name affinitas was first used in the sense of chemical relation by German philosopher Albertus Magnus near the year 1250. Those as Robert Boyle, John Mayow, Johann Glauber, Isaac Newton, Georg Stahl put forward ideas on elective affinity in attempts to explain how heat is evolved during combustion reactions; the term affinity has been used figuratively since c. 1600 in discussions of structural relationships in chemistry, etc. and reference to "natural attraction" is from 1616.
"Chemical affinity" has referred to the "force" that causes chemical reactions. As well as, more and earlier, the ″tendency to combine″ of any pair of substances; the broad definition, used throughout history, is that chemical affinity is that whereby substances enter into or resist decomposition. The modern term chemical affinity is a somewhat modified variation of its eighteenth-century precursor "elective affinity" or elective attractions, a term, used by the 18th century chemistry lecturer William Cullen. Whether Cullen coined the phrase is not clear, but his usage seems to predate most others, although it became widespread across Europe, was used in particular by the Swedish chemist Torbern Olof Bergman throughout his book De attractionibus electivis. Affinity theories were used in one way or another by most chemists from around the middle of the 18th century into the 19th century to explain and organise the different combinations into which substances could enter and from which they could be retrieved.
Antoine Lavoisier, in his famed 1789 Traité Élémentaire de Chimie, refers to Bergman's work and discusses the concept of elective affinities or attractions. According to chemistry historian Henry Leicester, the influential 1923 textbook Thermodynamics and the Free Energy of Chemical Reactions by Gilbert N. Lewis and Merle Randall led to the replacement of the term "affinity" by the term "free energy" in much of the English-speaking world. According to Prigogine, the term was developed by Théophile de Donder. Goethe used the concept in his novel Elective Affinities; the affinity concept was closely linked to the visual representation of substances on a table. The first-ever affinity table, based on displacement reactions, was published in 1718 by the French chemist Étienne François Geoffroy. Geoffroy's name is best known in connection with these tables of "affinities", which were first presented to the French Academy of Sciences in 1718 and 1720, as shown below: During the 18th century many versions of the table were proposed with leading chemists like Torbern Bergman in Sweden and Joseph Black in Scotland adapting it to accommodate new chemical discoveries.
All the tables were lists, prepared by collating observations on the actions of substances one upon another, showing the varying degrees of affinity exhibited by analogous bodies for different reagents. Crucially, the table was the central graphic tool used to teach chemistry to students and its visual arrangement was combined with other kinds diagrams. Joseph Black, for example, used the table in combination with chiastic and circlet diagrams to visualise the core principles of chemical affinity. Affinity tables were used throughout Europe until the early 19th century when they were displaced by affinity concepts introduced by Claude Berthollet. In chemical physics and physical chemistry, chemical affinity is the electronic property by which dissimilar chemical species are capable of forming chemical compounds. Chemical affinity can refer to the tendency of an atom or compound to combine by chemical reaction with atoms or compounds of unlike composition. In modern terms, we relate affinity to the phenomenon whereby certain atoms or molecules have the tendency to aggregate or bond.
For example, in the 1919 book Chemistry of Human Life physician George W. Carey states that, "Health depends on a proper amount of iron phosphate Fe32 in the blood, for the molecules of this salt have chemical affinity for oxygen and carry it to all parts of the organism." In this antiquated context, chemical affinity is sometimes found synonymous with the term "magnetic attraction". Many writings, up until about 1925 refer to a "law of chemical affinity". Ilya Prigogine summarized the concept of affinity, saying, "All chemical reactions drive the system to a state of equilibrium in which the affinities of the reactions vanish." The present IUPAC definition is that affinity A is the negative partial derivative of Gibbs free energy G with respect to extent of reaction ξ at constant pressure and temperature. That is, A = − P, T, it follows. In 1923, the Belgian mathematician and physicist Théophile de Donder derived a relation between affinity and the Gibbs free energy of a chem
Cambridge University Eco Racing
Cambridge University Eco Racing is the UK's leading solar car racing team. The team of 60 Cambridge students design and race solar-powered vehicles. Founded in 2007, their first prototype vehicle, became the first solar-powered car to drive on UK roads; the team compete in the biennial World Solar Challenge. CUER's race vehicle for the 2013 race, Resolution, is known for its innovative tracking plate design, unusual teardrop shape, its latest vehicle, builds upon this previous design and was entered into the 2015 race, where it became the best UK entry since 2007. Cambridge University Eco Racing is based in the University's Department of Engineering and comprises around 60 undergraduate members from several departments of Cambridge University; as well as having a large student body, the team is supported by a number of academic and industrial advisers, including Hermann Hauser and David Cleevely. The team was founded in 2007 by Martin McBrien, inspired by the solar car team at MIT, its first vehicle, was designed and constructed in early 2008 and was used as a prototype and display vehicle rather than for serious competition.
In June 2008, Affinity was driven from Land's End to John O'Groats to raise awareness of sustainable energy. As part of the End to End venture, it was endorsed by the Driver and Vehicle Licensing Agency to drive on UK roads, became the first such vehicle to qualify. CUER runs outreach events at local schools and has been featured in a wide range of local and international media. In July 2008, work began on Endeavour. Following design work by a number of students in the Engineering Department, with the support of the advisory board, the team competed in the 2009 World Solar Challenge, a 3000 km marathon across Australia, they came 14th, of 26 competitors, after a battery failure hindered their chances of competing effectively. Endeavour's 2009 entry was launched by Jenson Button at the Goodwood Festival of Speed. Over the next two years, they continued redesigning and refining Endeavour, resulting in a car with much improved aerodynamic properties and more reliable batteries; the team used CFD simulations to make minor tweaks to the canopy, tested the car extensively at a local airfield, before heading out to the next World Solar Challenge in October 2011.
There, after the hardest race on record due to a combination of thunderstorms and bush fires, they came 25th out of 37 teams. CUER's newest vehicle and Resolution's successor, was its entry into WSC 2015, it implements improvements that addresses many of the stability and structural problems that affected Revolution, while maintaining the new design. The race was used as a proof-of-concept for Evolution's design and to identify areas for improvement in future race cycles; as well as this, Evolution achieved 2,047 km on solar power to become the most successful UK entry into WSC since 2007 in terms of distance covered under solar power. The team finished 22nd of 27 Challenger class competitors. Affinity was CUER's first vehicle, built as a prototype and based on a shape taken from MIT's Manta Elite solar car. Affinity became the UK's first road legal solar car driving from Land's End to John o'Groats as part of CUER's "End to End" tour in 2008; the second generation vehicle and built to compete in the World Solar Challenge.
First entering the World Solar Challenge in 2009, the team led by Anthony Law raced across the Outback of Australia marking the teams highest placed finish to date. Endeavour was take to Australia again in 2011 by the team led by Emil Hewage. Designed and built in under 12 months, Resolution's innovative aerodynamic shape breaks away from the classic'table top' design seen in most entrants to the World Solar Challenge. Evolution formed an improvement to the design concept, pioneered with Resolution CUER attends industry conferences, they have been represented at the Raymond James’ 4th Annual European Investors North American Equities Conference, the Exhibition of Advanced Manufacturing and Engineering at Hethel Engineering Centre and Marketforce’s ‘Renewables 2008’. CUER exhibited in Cambridge at the ARM Partner Meeting, Cambridge Climate’s ‘Entrepreneurship for a Zero-Carbon Society’ conference and CIR’s ‘Solar Smart HEAT’ event. Further afield, CUER exhibited amongst the Europe’s top 100 Cleantech companies at the Guardian/Library House Essential Cleantech conference, presented at ‘Commercialising Photovoltaics’ organised by Renewables East.
List of solar car teams Cambridge University Eco Racing Website Cambridge University Engineering Department World Solar Challenge Varsity: "Cambridge Abroad", A. McNally, Dec 2008, p34 BlueSci: "Going Solar: Cambridge University Takes on the Solar Car Challenge", Jan 2009 p21 York Press Cambridge Evening News Yorkshire Post BBC News Financial Times Online 4Car HP.com East of England International BBC Cambridgeshire Sustainability: The Journal of Record Silicon.com Virgin Media Business Weekly BBC Radio York BBC Radio Scotland IOW Radio BBC Look East ITV Anglian News
An affinity group is a group formed around a shared interest or common goal, to which individuals formally or informally belong. Affinity groups are precluded from being under the aegis of any governmental agency, their purposes must be non-commercial. Examples of affinity groups include private social clubs, writing or reading circles, hobby clubs, groups engaged in political activism; some affinity groups are organized in a non-hierarchical manner using consensus decision making, are made up of trusted friends. They provide a method of organization, flexible and decentralized. Other affinity groups may have a hierarchy to provide management of the group's long-term interests, or if the group is large enough to require the delegation of responsibilities to other members or staff. Affinity groups can be based on a common ideology, a shared concern for a given issue or a common activity, interest or skill. Affinity groups may have either closed membership, although the latter is far more common.
Some expect members to share the cost of the group's expenses. Although affinity groups are a natural way for humans to organize and are, in that sense, as old as humanity, the origin of affinity groups in the current context began in the 16th century in Britain with dining clubs that would meet at a set location and at a recurring time. One of the earliest recorded examples of such was a group that called itself the "Fraternity of Sireniacal Gentlemen" which met at the Mermaid Tavern in London the first Friday night of each month. Membership was limited and many of the Elizabethan Era's most prominent literary figures belonged, they gathered to eat and socialize with other members, to discuss literary matters. During the 17th century, far more affinity groups formed, ranging from large, national or international fraternal groups like the Freemasons to private gentlemen's clubs, to small, informal reading circles or collectors clubs. Unlike salons or other periodic gatherings that had continuously changing participants, affinity groups traditionally have had curated memberships.
A would-be member had to be proposed for membership by an existing member, or would-be members might petition to join on their own. The existing members are required to vote upon whether or not to accept the applicant as a new member; some voting procedures require unanimity, others may require a simple majority of supporting votes. After becoming a member, continuing membership may be contingent upon conforming to rules or shared ideologies, the disbarring of members for a variety of reasons is possible. Affinity groups fall under the category of NGOs, but are further limited by being non-commercial, are not required to have any specific purpose that might affect the community beyond their own group. For example, both a social justice group and a philately group would be considered affinity groups, but the former more resembles the classic definition of an NGO. Affinity groups engaged in political activism date to 19th century Spain, it was a favourite way of organization by Spanish anarchists, had their base in the tertulias or in the local groups.
Politically oriented affinity groups in the United States gained public attention during the anti-Vietnam War movement of the 1960s and 1970s. The term was first used by the group Black Mask. Anti-war activists on college campuses organized around their hobbies or backgrounds -- religious, ethnic group, etc, they became popular in the 1970s in the anti-nuclear movement in the United States and Europe. The 30,000 person occupation and blockade of the Ruhr nuclear power station in Germany in 1969 was organized on the Affinity group model. Today, the structure is used by many different activists: animal rights, anti-war, anti-globalization, to name some examples; the 1999 protests in Seattle which shut down the WTO Ministerial Conference of 1999 included coordinated organization by many clusters of Affinity groups. By definition, Affinity groups are autonomous from any larger body. Co-ordinated effort and co-operation amongst several Affinity groups, however, is achieved by using a loose form of confederation.
Private clubs, for example, may cooperate through reciprocal agreements which allow the members of one club to use the facilities of another club in a different location. Other affinity groups, such as Rotarians or Toastmasters, may be individual units that conform to shared standards so that one may participate in another group of the same name anywhere on earth without requiring the individual to reapply for a new membership. Cluster: The cluster is the basic unit of organization amongst Affinity groups. A cluster is organized in a non-hierarchical manner. A cluster can be permanent, but is more an ad hoc grouping organized for one specific task or action. One can be organized around a common ideology or a place of origin. Spokescouncil: The spokescouncil is an aggregate of clusters and Affinity groups; each Affinity group or cluster nominates one representative to participate in the council. Spokescouncils are most temporary bodies, committed to accomplishing one task or event. Affinity groups tend to be loosely organized, however there are some formal roles or positions that occur.
A given Affinity group may have some or none of these positions. They may be permanent or temporary and the group may opt to take turns in