Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation, biologically functional, in an expeditious and reproducible manner. It is the physical process by which a polypeptide folds into its characteristic and functional three-dimensional structure from a random coil; each protein exists as an unfolded polypeptide or random coil when translated from a sequence of mRNA to a linear chain of amino acids. This polypeptide lacks any stable three-dimensional structure; as the polypeptide chain is being synthesized by a ribosome, the linear chain begins to fold into its three-dimensional structure. Folding begins to occur during translation of the polypeptide chain. Amino acids interact with each other to produce a well-defined three-dimensional structure, the folded protein, known as the native state; the resulting three-dimensional structure is determined by the amino acid sequence or primary structure. The correct three-dimensional structure is essential to function, although some parts of functional proteins may remain unfolded, so that protein dynamics is important.

Failure to fold into native structure produces inactive proteins, but in some instances misfolded proteins have modified or toxic functionality. Several neurodegenerative and other diseases are believed to result from the accumulation of amyloid fibrils formed by misfolded proteins. Many allergies are caused by incorrect folding of some proteins, because the immune system does not produce antibodies for certain protein structures. Denaturation of proteins is a process of transition from the folded to the unfolded state, it happens in cooking, in burns, in proteinopathies, in other contexts. The duration of the folding process varies depending on the protein of interest; when studied outside the cell, the slowest folding proteins require many minutes or hours to fold due to proline isomerization, must pass through a number of intermediate states, like checkpoints, before the process is complete. On the other hand small single-domain proteins with lengths of up to a hundred amino acids fold in a single step.

Time scales of milliseconds are the norm and the fastest known protein folding reactions are complete within a few microseconds. The primary structure of a protein, its linear amino-acid sequence, determines its native conformation; the specific amino acid residues and their position in the polypeptide chain are the determining factors for which portions of the protein fold together and form its three-dimensional conformation. The amino acid composition is not as important as the sequence; the essential fact of folding, remains that the amino acid sequence of each protein contains the information that specifies both the native structure and the pathway to attain that state. This is not to say. Conformations differ based on environmental factors as well. Formation of a secondary structure is the first step in the folding process that a protein takes to assume its native structure. Characteristic of secondary structure are the structures known as alpha helices and beta sheets that fold because they are stabilized by intramolecular hydrogen bonds, as was first characterized by Linus Pauling.

Formation of intramolecular hydrogen bonds provides another important contribution to protein stability. Α-helices are formed by hydrogen bonding of the backbone to form a spiral shape. The β pleated sheet is a structure that forms with the backbone bending over itself to form the hydrogen bonds; the hydrogen bonds are between the amide carbonyl oxygen of the peptide bond. There exists anti-parallel β pleated sheets and parallel β pleated sheets where the stability of the hydrogen bonds is stronger in the anti-parallel β sheet as it hydrogen bonds with the ideal 180 degree angle compared to the slanted hydrogen bonds formed by parallel sheets; the alpha helices and beta pleated sheets can be amphipathic in nature, or contain a hydrophilic portion and a hydrophobic portion. This property of secondary structures aids in the tertiary structure of a protein in which the folding occurs so that the hydrophilic sides are facing the aqueous environment surrounding the protein and the hydrophobic sides are facing the hydrophobic core of the protein.

Secondary structure hierarchically gives way to tertiary structure formation. Once the protein's tertiary structure is formed and stabilized by the hydrophobic interactions, there may be covalent bonding in the form of disulfide bridges formed between two cysteine residues. Tertiary structure of a protein involves a single polypeptide chain. Tertiary structure may give way to the formation of quaternary structure in some proteins, which involves the "assembly" or "coassembly" of subunits that have folded. Folding is a spontaneous process, guided by hydrophobic interactions, formation of intramolecular hydrogen bonds, van der Waals forces, it is opposed by conformational entropy; the process of folding begins co-translationally, so that the N-terminus of the protein begins to fold while the C-terminal portion of the protein is still being synthesized by the ribosome. While these macro

Ho Jong-suk was a Korean independence activist, writer and communist. Her real name was Jongja, she was a member of Singanhoe and the Communist Party of Korea and an early Korean women's rights activist. In her early years, Ho went to Japan to study in Kwansei School in Tokyo, she left and in her next years Ho went to China where she was given an entrance to Shanghai Foreign High School where she graduated. She returned to her country. In 1921, she joined Korean Communist Party. At that time, Japanese Government-General of Korea decided to make the Communist Party illegal, she avoided persecution for participation in the Communist Party. In 1924, she was introduced to International Women's Day, on March 1925, she went to Women's Day event in Seoul. In 1927 she was a founding member of Geunwoohoi and participated to Singanhoe. Ho was in favor of "Unrelated Love and Sex", her opinion was denounced in Korean society because at that time, the vestiges of fundamentalist Confucianism remained in the Koreas.

In 1936, she went to China. In 1938, she went to Hebei, participated in Chosen Independence alliance, an Anti-Japanese Korean resistance Group. In 1945, she went to Seoul but she left for North Korea to avoid right wing terrorism. In 1948 she participated in the North Korean government. Ho served as the Chief Justice of the Supreme Court of North Korea between 28 October 1959 and 1960. In Grace Lover Democraticism founder days Historical rememories of great loves Hwang Jini Heo Nanseolheon Na Hye-sok Shin Saimdang Ho Jong-suk:britannica Ho Jong-suk Ho Jong-suk Ho Jong-suk Ho Jong-suk 조선의 첫 녀성상

The Reid Memorial Church is a church in Edinburgh. It is a congregation of the Church of Scotland and is located in the Blackford area on the south side of the city. After growing resentment within the Church of Scotland about the appointment of ministers by the patron of a church, the Disruption of 1843 led to the Free Church of Scotland. Among the ministers seceding was Dr. Robert Gordon of St Giles', he became the first minister of the "Free High" congregation. After he died in 1853, he was succeeded by Robert Rainy, minister until 1862, followed by other eminent preachers and scholars; the United Free Church of Scotland was formed in 1900 when the Free Church combined with the United Presbyterian Church, which rejoined the Church of Scotland in 1929. William Reid was a successful Edinburgh businessman during the 19th century, when he died in 1889 he left his wealth to his four sons; the last son, William Crambe Reid, died without heirs in 1921 after inheriting the wealth of his brothers, bequeathed his estate to the United Free Church to build a church in memory of his father, but the reunion of the churches had taken place before construction started.

There being an abundance of churches in the south side of Edinburgh, the Presbytery of Edinburgh moved the congregation of the Free High Church attached to the New College at the top of The Mound into the new building, as their building was to be used for the expansion of the activities of the College. It was dedicated on 3 January 1935, the first Sunday service, on 6 January, was officiated by Rev. J Marshall Robertson. On June 11, 2019, the Rev. Alex McAspurren was inducted as minister of both Craigmillar Park Church and Reid Memorial Church, the two churches having been linked by the Presbytery of Edinburgh the previous year; the church was designed by Leslie Grahame Thomson and built between 1929 and 1933. It is in an Arts and Crafts Gothic style, replicating mediaeval churches with cathedral-like proportions and layout, it consists of a cruciform with a square tower to the south-east. To the east of this main section is a cloister court, around which are arranged vestries, the session house, a hall and the church officer's house.

The windows along the side are decorated with tracery and there are flanking buttresses that travel above the height of the windows. The three windows of the chancery are decorated with stained glass by James Ballantine, depicting the Nativity and Ascension; the Church is located in a triangular area between West Savile Terrace to the north, Blackford Avenue to the south, a steep hill that rises above it. It was protected as a category A listed building on 12 December 1974; the organ was built by Rushworth and Dreaper