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Alpha helix

The alpha helix is a common motif in the secondary structure of proteins and is a right hand-helix conformation in which every backbone N−H group hydrogen bonds to the backbone C=O group of the amino acid located three or four residues earlier along the protein sequence. The alpha helix is called a classic Pauling–Corey–Branson α-helix; the name 3.613-helix is used for this type of helix, denoting the average number of residues per helical turn, with 13 atoms being involved in the ring formed by the hydrogen bond. Among types of local structure in proteins, the α-helix is the most extreme and the most predictable from sequence, as well as the most prevalent. In the early 1930s, William Astbury showed that there were drastic changes in the X-ray fiber diffraction of moist wool or hair fibers upon significant stretching; the data suggested that the unstretched fibers had a coiled molecular structure with a characteristic repeat of ≈5.1 ångströms. Astbury proposed a kinked-chain structure for the fibers.

He joined other researchers in proposing that: the unstretched protein molecules formed a helix the stretching caused the helix to uncoil, forming an extended state. Although incorrect in their details, Astbury's models of these forms were correct in essence and correspond to modern elements of secondary structure, the α-helix and the β-strand, which were developed by Linus Pauling, Robert Corey and Herman Branson in 1951. Hans Neurath was the first to show that Astbury's models could not be correct in detail, because they involved clashes of atoms. Neurath's paper and Astbury's data inspired H. S. Taylor, Maurice Huggins and Bragg and collaborators to propose models of keratin that somewhat resemble the modern α-helix. Two key developments in the modeling of the modern α-helix were: the correct bond geometry, thanks to the crystal structure determinations of amino acids and peptides and Pauling's prediction of planar peptide bonds; the pivotal moment came in the early spring of 1948, when Pauling went to bed.

Being bored, he drew a polypeptide chain of correct dimensions on a strip of paper and folded it into a helix, being careful to maintain the planar peptide bonds. After a few attempts, he produced a model with physically plausible hydrogen bonds. Pauling worked with Corey and Branson to confirm his model before publication. In 1954, Pauling was awarded his first Nobel Prize "for his research into the nature of the chemical bond and its application to the elucidation of the structure of complex substances", prominently including the structure of the α-helix; the amino acids in an α-helix are arranged in a right-handed helical structure where each amino acid residue corresponds to a 100° turn in the helix, a translation of 1.5 Å along the helical axis. Dunitz describes how Pauling's first article on the theme in fact shows a left-handed helix, the enantiomer of the true structure. Short pieces of left-handed helix sometimes occur with a large content of achiral glycine amino acids, but are unfavorable for the other normal, biological L-amino acids.

The pitch of the alpha-helix is 5.4 Å, the product of 1.5 and 3.6. What is most important is that the N-H group of an amino acid forms a hydrogen bond with the C=O group of the amino acid four residues earlier. Official international nomenclature specifies two ways of defining α-helices, rule 6.2 in terms of repeating φ, ψ torsion angles and rule 6.3 in terms of the combined pattern of pitch and hydrogen bonding. The α-helices can be identified in protein structure using several computational methods, one of, DSSP. Similar structures include the π-helix; the α-helix can be described as a 3.613 helix, since the i + 4 spacing adds three more atoms to the H-bonded loop compared to the tighter 310 helix, on average, 3.6 amino acids are involved in one ring of α-helix. The subscripts refer to the number of atoms in the closed loop formed by the hydrogen bond. Residues in α-helices adopt backbone dihedral angles around, as shown in the image at right. In more general terms, they adopt dihedral angles such that the ψ dihedral angle of one residue and the φ dihedral angle of the next residue sum to −105°.

As a consequence, α-helical dihedral angles, in general, fall on a diagonal stripe on the Ramachandran diagram, ranging from to. For comparison, the sum of the dihedral angles for a 310 helix is −75°, whereas that for the π-helix is −130°; the general formula for the rotation angle Ω per residue of any polypeptide helix with trans isomers is given by the equation 3 cos Ω = 1 − 4 cos2 φ + ψ/2The α-helix is packed. The amino-acid side-chains are on the outside of the helix, point "downward", like the branches of an evergreen tree; this directionality is sometimes used in preliminary, low-resolution electron-density maps to determine the direction


CFBR-FM is a Canadian radio station, broadcasting an active rock format at 100.3 on the FM dial in Edmonton, Alberta. The station is owned by Bell Media; the station was launched in 1951 by Sunwapta Broadcasting as CFRN-FM, simulcasting the AM programming of CFRN. It launched separate programming in 1964, adopted the callsign CKXM in 1979; the station was adopted the callsign CJKE the following year. The station adopted the current CFBR callsign. On September 28, 2007, the CRTC approved the sale of CFBR and all Standard Radio assets to Astral Media. On June 27, 2013, the CRTC approved the sale of all but 10 Astral Media Radio Stations to BCE; the sale including CFBR. The Bear is rebroadcast in Jasper on 92.3 FM. In 2008, CFBR was rated as the third most listened-to station in the Edmonton market, but by the Fall 2011 book, it had dropped to #6. CFBR used to be the call sign of an AM station in Brockville, known today as CFJR, was a call sign of an AM radio station in Sudbury, now known as CHYC-FM.

Official website CFBR-FM history – Canadian Communications Foundation Query the REC Canadian station database for CFBR-FM

Wayland Becker

Wayland Herman Becker was an American football player. He played in the National Football League for six seasons. Becker was born in Soperton and attended East High School in Green Bay, Wisconsin. While in high school, he twice led his football team to Fox River Valley conference championships, in 1928 and 1929. Becker went on to attend Marquette University, where he played football and basketball, lettering twice. Becker began his NFL career with the George Halas's Chicago Bears in 1934, he played just two games for the Bears before completing the 1934 season with the Brooklyn Dodgers, with whom he stayed through the 1935 season. In 1936 Becker went to the Green Bay Packers; those Packers teams played in the NFL Championship Game twice during his tenure, winning in 1936 and losing in 1938. He finished his NFL career in 1939 with the Pittsburgh Pirates, he was released by the Pirates after two games. In 1941 he turned up on the Columbus Bullies of the American Football League; the team won the AFL championship and Becker was named by the league's coaches as second-team All-League based on his performance that season.

Wayland Becker at Find a Grave

Sweet (Ken Mellons album)

Sweet is the fourth studio album released by American country music artist Ken Mellons. Released in 2004, it contains the song "Paint Me a Birmingham", recorded by Tracy Lawrence and released as a single. Mellons's rendition was released shortly before Lawrence's. "Smack Dab" was recorded by George Jones on his 1998 album It Don't Get Any Better Than This. "Smack Dab" – 3:02 "Just What I'm Wantin' to Do" – 2:56 "Paint Me a Birmingham" – 3:48 "Climb My Tree" – 2:33 "Interstate Gypsy" – 3:23 "You Can't Make My Heart Believe" – 3:39 "Sweet" – 4:00 "All I Need Is a Bridge" – 4:24 "Single Again" – 2:37 "Any Time, Any Place" – 3:11 "Institute of Honky Tonks" – 3:03 Duet with George Jones "If I've Learned Anything at All" – 2:35 Mike Chapman - bass guitar Larry Cordle - background vocals Glen Duncan - fiddle Terry Eldredge - background vocals Larry Franklin - fiddle Vince Gill - background vocals Owen Hale - drums Wes Hightower - background vocals Rebecca Lynn Howard - background vocals Bill Hullett - acoustic guitar Carl Jackson - banjo George Jones - background vocals Liana Manis - background vocals Brent Mason - electric guitar Ken Mellons - lead vocals Gordon Mote - keyboards John Wesley Ryles - background vocals Scotty Sanders - steel guitar Earl Scruggs - banjo Steve Turner - drums Sweet at Allmusic

Robert Anderson (New Zealand politician)

Robert Arnold Anderson was a New Zealand politician. He was a National Party MP from 1987 to 1996. Anderson was born in Epsom, England on 22 January 1936, educated in England and Southern Rhodesia, he was a member of the Local Government Commission. He was first elected to Parliament in the 1987 election as MP for Kaimai, he left Parliament at the 1996 election. He had been selected as National candidate for the new seat of Coromandel which replaced Kaimai, but withdrew due to illness, he was replaced by Murray McLean, who lost in the 1999 election. Anderson was awarded the New Zealand 1990 Commemoration Medal, he died at Mount Maunganui on 24 October 1996. Temple, Philip. Temple's Guide to the 44th New Zealand Parliament. Dunedin: McIndoe Publishers. P. 53. ISBN 0 86868 159 8. 1990 Parliamentary Candidates for the New Zealand National Party by John Stringer

Vasilashki Lakes

The Vasilashki Lakes are situated in Pirin, Bulgaria in a large cirque between the Todorka and Vasilashki Chukar peaks. The cirque is opened to the east, where it faces the Demyanitsa river in which the water of the lakes pour; this cirque includes the two lakes Todorini Ochi, whose waters goes to one of the Vasilaski lakes. The cirque is amphitheatric and in fact consists of several smaller cirques situated in a fan-shape way above the main one, in which the two largest lakes are located; the lakes are 10 including the two Todorini, with a total surface area of 160 decares. Their name derives from the legent for Vasil, the beloved one of Todorka, who plunged into the Fish Vasilashko lake when she broke his heart; the most important lakes are: The Tevno Vasilashko Lake, called the Blue Lake is one of the largest and deepest lakes in the mountain, is first by these indicators in the group. It is situated at an altitude of 2,362 m; the water volume of 510,000 m³ is considerable and is third in Pirin.

The lake has exceptional beauty, saturated a tiny islet in the middle. The water pours out in the Upper Vasilashko Lake by means of underground stream, which makes it impossible for the fish to reach it; the Fish Vasilashko Lake, sometimes referred as the Big Vasilashko Lake, is second in size and is situated below the Upper Lake at 2,126 m. It is 325 m long and 177 m wide with maximum depth of 2.5 m, which explains its small volume-only 41,000 m³. A small picturesque peninsular juts out in its southern part; the lake gathers the water of the whole cirque. At first, it forms an underground river under the ridge but at a distance of 250 m the waters appear on the surface and sweeps down the slopes; the lake teems with trout, which has given its name. The Upper Vasilashko Lake is situated at 2,154 m under the Tipits Peak, its shape has area of 23.2 decares. It is not deep: only 3.1 m and the volume is 29,000 m³. It is the place where the water from the Todora's Eyes and Tevnoto Lake pour in; the Rainbow-shaped Vasilashko Lake is situated in a separate small cirque under the Tipits Peak at 2,215 m.

With depth of 10.4 m, it is second in ninth in Pirin. It is not large: its surface is only 10.9 decares. The lake has a shape of an irregular pentagonal, its water pour into the Fish Lake under the ground. The Upper Todorino Lake is the larger of the two lakes of the same name. Situated at 2,536 m it is among of the highest in Pirin; this is. The surface area is 13.2 decares. It is perfectly round with size of 124x151 m; the two lakes are famous as the Todora's Eyes to remember the maiden Todorka who bewailed her beloved Vasil and her tears created the lakes. The Lower Todorino Lake is located at 2,510 m, its surface area is 6.7 decares. It is almost round: 110x82 m