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3 10 Helix
A 310 helix is a type of secondary structure found in proteins and polypeptides. Of the numerous protein secondary structures present, the 310-helix is the fourth most common type observed; following α-helices, β-sheets and reverse turns. 310-helices constitute nearly 10–15% of all helices in protein secondary structures, and are typically observed as extensions of α-helices found at either their N- or C- termini. Because of the α-helices tendency to consistently fold and unfold, it has been proposed that the 310-helix serves as an intermediary conformation of sorts, and provides insight into the initiation of α-helix folding. Discovery Max Perutz, the head of the Medical Research Council Laboratory of Molecular Biology at the University of Cambridge, wrote the first paper documenting the elusive 310-helix. Together with Lawrence Bragg and John Kendrew, Perutz published an exploration of polypeptide chain configurations in 1950, based on cues from noncrystalline d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
3 10 Helix Neg49 Neg26 Sideview
3 (three) is a number, numeral and digit. It is the natural number following 2 and preceding 4, and is the smallest odd prime number and the only prime preceding a square number. It has religious and cultural significance in many societies. Evolution of the Arabic digit The use of three lines to denote the number 3 occurred in many writing systems, including some (like Roman and Chinese numerals) that are still in use. That was also the original representation of 3 in the Brahmic (Indian) numerical notation, its earliest forms aligned vertically. However, during the Gupta Empire the sign was modified by the addition of a curve on each line. The Nāgarī script rotated the lines clockwise, so they appeared horizontally, and ended each line with a short downward stroke on the right. In cursive script, the three strokes were eventually connected to form a glyph resembling a with an additional stroke at the bottom: ३. The Indian digits spread to the Caliphate in the 9th c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DNA Double Helix
In molecular biology, the term double helix refers to the structure formed by double-stranded molecules of nucleic acids such as DNA. The double helical structure of a nucleic acid complex arises as a consequence of its secondary structure, and is a fundamental component in determining its tertiary structure. The structure was discovered by Rosalind Franklin and her student Raymond Gosling, Maurice Wilkins, James Watson, and Francis Crick, while the term "double helix" entered popular culture with the 1968 publication of Watson's '' The Double Helix: A Personal Account of the Discovery of the Structure of DNA''. The DNA double helix biopolymer of nucleic acid is held together by nucleotides which base pair together. In B-DNA, the most common double helical structure found in nature, the double helix is right-handed with about 10–10.5 base pairs per turn. The double helix structure of DNA contains a ''major groove'' and ''minor groove''. In B-DNA the major groove is wider ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Voltage-gated Potassium Channel
Voltage-gated potassium channels (VGKCs) are potassium channel, transmembrane channels specific for potassium and Voltage-gated ion channel, sensitive to voltage changes in the cell's membrane potential. During action potentials, they play a crucial role in returning the depolarized cell to a resting state. Classification Alpha subunits Alpha subunits form the actual conductance pore. Based on sequence homology of the hydrophobic transmembrane cores, the alpha subunits of voltage-gated potassium channels are grouped into 12 classes. These are labeled Kvα1-12. The following is a list of the 40 known human voltage-gated potassium channel alpha subunits grouped first according to function and then subgrouped according to the Kv sequence homology classification scheme: Delayed rectifier slowly inactivating or non-inactivating *Kvα1.x - shaker superfamily of potassium channels, Shaker-related: Kv1.1 (KCNA1), Kv1.2 (KCNA2), Kv1.3 (KCNA3), Kv1.5 (KCNA5), Kv1.6 (KCNA6), Kv1.7 (KCN ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Trends Biochem
A fad, trend, or craze is any form of collective behavior that develops within a culture, a generation, or social group in which a group of people enthusiastically follow an impulse (psychology), impulse for a short time period. Fads are Subject and object (philosophy), objects or behaviors that achieve short-lived popularity but fade away. Fads are often seen as sudden, quick-spreading, and short-lived events. Fads include fad diet, diets, clothing, hairstyles, toys, and more. Some popular fads throughout history are toys such as yo-yos, hula hoops, and fad dances such as the Macarena (song), Macarena, Floss (dance), floss and the Twist (dance), twist. Similar to habits or Convention (norm), customs but less durable, fads often result from an activity or behavior being perceived as Popularity, popular or excited state, exciting within a peer group, or being deemed "peer pressure, cool" as often promoted by social networks.Kornblum (2007), p. 213. A fad is said to "catch on" wh ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Globular Protein
In biochemistry, globular proteins or spheroproteins are spherical ("globe-like") proteins and are one of the common protein types (the others being fibrous, disordered and membrane proteins). Globular proteins are somewhat water-soluble (forming colloids in water), unlike the fibrous or membrane proteins. There are multiple fold classes of globular proteins, since there are many different architectures that can fold into a roughly spherical shape. The term globin can refer more specifically to proteins including the globin fold. Globular structure and solubility The term globular protein is quite old (dating probably from the 19th century) and is now somewhat archaic given the hundreds of thousands of proteins and more elegant and descriptive structural motif vocabulary. The globular nature of these proteins can be determined without the means of modern techniques, but only by using ultracentrifuges or dynamic light scattering techniques. The spherical structure is induce ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
World Scientific Publishing
World Scientific Publishing is an academic publisher of scientific, technical, and medical books and journals headquartered in Singapore. The company was founded in 1981. It publishes about 600 books annually, with more than 170 journals in various fields. In 1995, World Scientific co-founded the London-based Imperial College Press together with the Imperial College of Science, Technology and Medicine. Company structure The company head office is in Singapore. The Chairman and Editor-in-Chief is Dr Phua Kok Khoo, while the Managing Director is Doreen Liu. The company was co-founded by them in 1981. Imperial College Press In 1995 the company co-founded Imperial College Press, specializing in engineering, medicine and information technology, with Imperial College London Imperial College London, also known as Imperial, is a Public university, public research university in London, England. Its history began with Prince Albert of Saxe-Coburg and Gotha, Prince Albert, h ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Haemoglobin
Hemoglobin (haemoglobin, Hb or Hgb) is a protein containing iron that facilitates the transportation of oxygen in red blood cells. Almost all vertebrates contain hemoglobin, with the sole exception of the fish family Channichthyidae. Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers an animal's metabolism. A healthy human has 12to 20grams of hemoglobin in every 100mL of blood. Hemoglobin is a metalloprotein, a chromoprotein, and a globulin. In mammals, hemoglobin makes up about 96% of a red blood cell's dry weight (excluding water), and around 35% of the total weight (including water). Hemoglobin has an oxygen-binding capacity of 1.34mL of O2 per gram, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood plasma alone. The mammalian hemoglobin molecule can bind and transport up to four oxygen ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Myoglobin
Myoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the cardiac and skeletal muscle, skeletal Muscle, muscle tissue of vertebrates in general and in almost all mammals. Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not have cooperative binding with oxygen like hemoglobin does. Myoglobin consists of non-polar amino acids at the core of the globulin, where the heme group is non-covalently bounded with the surrounding polypeptide of myoglobin. In humans, myoglobin is found in the bloodstream only after Strain (injury), muscle injury. (Google books link is the 2008 edition) High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin. Myoglobin is found in Type I muscle, Type II A, and Type II B; although many older texts describe myo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gibbs Free Energy
In thermodynamics, the Gibbs free energy (or Gibbs energy as the recommended name; symbol is a thermodynamic potential that can be used to calculate the maximum amount of Work (thermodynamics), work, other than Work (thermodynamics)#Pressure–volume work, pressure–volume work, that may be performed by a closed system, thermodynamically closed system at constant temperature and pressure. It also provides a necessary condition for processes such as chemical reactions that may occur under these conditions. The Gibbs free energy is expressed as G(p,T) = U + pV - TS = H - TS where: * U is the internal energy of the system * H is the enthalpy of the system * S is the entropy of the system * T is the temperature of the system * V is the volume of the system * p is the pressure of the system (which must be equal to that of the surroundings for mechanical equilibrium). The Gibbs free energy change (, measured in joules in International System of Units, SI) is the ''maximum'' amount of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Condensation Reaction
In organic chemistry, a condensation reaction is a type of chemical reaction in which two molecules are combined to form a single molecule, usually with the loss of a small molecule such as water. If water is lost, the reaction is also known as a dehydration synthesis. However other molecules can also be lost, such as ammonia, ethanol, acetic acid and hydrogen sulfide. The addition of the two molecules typically proceeds in a step-wise fashion to the addition product, usually in equilibrium, and with loss of a water molecule (hence the name condensation). The reaction may otherwise involve the functional groups of the molecule, and is a versatile class of reactions that can occur in acidic or basic conditions or in the presence of a catalyst. This class of reactions is a vital part of life as it is essential to the formation of peptide bonds between amino acids and to the biosynthesis of fatty acids. Many variations of condensation reactions exist. Common examples include ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amino Acid
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. Only these 22 appear in the genetic code of life. Amino acids can be classified according to the locations of the core structural functional groups ( alpha- , beta- , gamma- amino acids, etc.); other categories relate to polarity, ionization, and side-chain group type ( aliphatic, acyclic, aromatic, polar, etc.). In the form of proteins, amino-acid '' residues'' form the second-largest component (water being the largest) of human muscles and other tissues. Beyond their role as residues in proteins, amino acids participate in a number of processes such as neurotransmitter transport and biosynthesis. It is thought that they played a key role in enabling life on Earth and its emergence. Amino acids are formally named by the IUPAC- IUBMB Joint Commi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Amide
In organic chemistry, an amide, also known as an organic amide or a carboxamide, is a chemical compound, compound with the general formula , where R, R', and R″ represent any group, typically organyl functional group, groups or hydrogen atoms. The amide group is called a peptide bond when it is part of the Polymer backbone, main chain of a protein, and an isopeptide bond when it occurs in a side chain, as in asparagine and glutamine. It can be viewed as a Derivative (chemistry), derivative of a carboxylic acid () with the hydroxyl group () replaced by an amino group (); or, equivalently, an acyl group, acyl (alkanoyl) group () joined to an amino group. Common amides are formamide (), acetamide (), benzamide (), and dimethylformamide (). Some uncommon examples of amides are ''N''-chloroacetamide () and chloroformamide (). Amides are qualified as primary (chemistry), primary, secondary (chemistry), secondary, and tertiary (chemistry), tertiary according to the number of acyl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
