PBB geneid 4151 Myoglobin is an iron and oxygen binding protein found in the muscle tissue of vertebrates ... binding protein in blood, specifically in the red blood cells. The only time myoglobin is found in the bloodstream ... 2000 page 206 edition 3rd isbn 071676203X ref Myoglobin abbreviated Mb is a tertiary structure single ... pigment of muscle tissues. ref name review cite journal title Myoglobin an essential hemoprotein in striated ... www.ncbi.nlm.nih.gov entrez query.fcgi?cmd Search&db books&doptcmdl GenBookHL&term myoglobin AND mcb ... family members myoglobin and hemoglobin title Molecular Cell Biology edition 4th author Harvey .... Instead, the binding of oxygen by myoglobin is unaffected by the oxygen pressure in the surrounding tissue. Myoglobin is often cited as having an instant binding tenacity to oxygen given its hyperbolic oxygen Dissociation chemistry dissociation curve. High concentrations of myoglobin in muscle cells ... with particularly high myoglobin abundance. ref name Nelson00 Myoglobin was the first protein to have ... ref In 1958, John Kendrew and associates successfully determined the structure of myoglobin by high ... of the Myoglobin Molecule Obtained by X Ray Analysis author JC Kendrew, G Bodo, HM Dintzis, RG Parrish ... physiological function is not yet conclusively established mice genetically engineered to lack myoglobin ... Hypoxia induced left ventricular dysfunction in myoglobin deficient mice author Mammen PP, Kanatous ... ajpheart.00147.2003 ref In humans myoglobin is encoded by the MB gene . ref name pmid2989088 cite journal author Akaboshi E title Cloning of the human myoglobin gene journal Gene volume 33 issue 3 pages ... thumb left An X ray diffraction image for the protein myoglobinMyoglobin forms pigment s responsible ... states of the iron atom in myoglobin and the oxygen species attached to it. When meat is in its ... 535 story 1518775.html ref Myoglobin is found in Type I muscle, Type II A and Type II B, but most texts consider myoglobin not to be found in smooth muscle. Role in disease Myoglobin is released ... more details
Orphan date February 2009 A coboglobin is a synthetic compound, a metalloprotein chemically similar to hemoglobin or myoglobin but using the metal cobalt instead of iron hence the name . Just like hemoglobin and myoglobin, the coboglobins are able to reversibly bind molecular oxygen O sub 2 sub at the metal atom. However they lose this ability much faster than the natural molecules . Blood of this type would be amber yellow in colour when in the veins while uncoloured and clear in the arteries . References B. M. Hoffman, D. H. Petering. Coboglobins Oxygen Carrying Cobalt Reconstituted Hemoglobin and Myoglobin. Proceedings of the National Academy of Sciences of the United States of America , Vol. 67, No. 2 Oct. 15, 1970 , pp. 637 643 Category Metalloproteins ru ... more details
Infobox disease Name Myoglobinuria Image Myoglobin.png Caption Model of helical domains in myoglobin. DiseasesDB 23059 ICD10 ICD10 R 82 1 r 80 ICD9 ICD9 791.3 ICDO OMIM MedlinePlus eMedicineSubj ped eMedicineTopic 1535 MeshID D009212 Myoglobinuria is the presence of myoglobin in the urine , usually associated with rhabdomyolysis or muscle destruction. Myoglobin is present in muscle cells as a reserve of oxygen . Causes Physical trauma Trauma , vascular problems, venom s, certain drugs and other situations can destroy or damage the muscle, releasing myoglobin to the circulation and thus to the kidneys. Under ideal situations myoglobin will be filtered and excreted with the urine, but if too much myoglobin is released into the circulation or in case of renal problems, it can occlude the renal filtration system leading to acute tubular necrosis and acute renal insufficiency . Other causes of myoglobinuria include McArdle s disease Phosphofructokinase deficiency ref name pmid18421897 cite journal author Toscano A, Musumeci O title Tarui disease and distal glycogenoses clinical and genetic update journal Acta Myol volume 26 issue 2 pages 105 7 year 2007 month October pmid 18421897 doi url issn ref Carnitine palmitoyltransferase II deficiency Diagnosis After centrifuging, the serum of myoglobinuria is clear, where the serum of hemoglobinuria after centrifuge is pink. Citation needed date January 2008 External links http neuromuscular.wustl.edu msys myoglob.html Overview on the Neuromuscular disease center website. References reflist Abnormal clinical and laboratory findings for urine Category Abnormal clinical and laboratory findings for urine disease stub de Myoglobinurie ru ... more details
Unreferenced date August 2007 A meat slurry , reconstituted meat , or emulsified meat is a liquefied meat product that contains fewer fats, pigments and less myoglobin than unprocessed dark meat s. Meat slurry also eases the process of meat distribution and is more malleable than dark meats. Meat slurry is not designed to sell for general consumption rather, it is used as a meat supplement in food products for humans, such as chicken nuggets , and food for domestic animals. Poultry is the most common meat slurry however, beef and pork are also used. Properties and production Dark meat from poultry is often viewed as less palatable in Western countries because of its color, low plasticity and high fat content. Dubious date February 2010 These characteristics are caused by myoglobin, a pigmented chemical compound found in muscle tissue that undergoes frequent use. Because domestic poultry rarely fly, the flight muscles in the breast contain little myoglobin and appear white. Dark meat which is high in myoglobin is less useful in industry, especially fast food , because it is difficult to mold into shapes. Processing dark meat into a slurry makes it more like white meat, easier to prepare and more attractive. The meat is first finely ground and mixed with water. The mixture is then used in a centrifuge or with an emulsifier to separate the fats and myoglobin from the muscle. The product is then allowed to settle into three layers meat, excess water, and fat. The remaining liquefied meat is then Flash freezing flash frozen and packaged. See also Mechanically separated meat Offal External links http www.uga.edu news artman publish 050809fletcher.shtml UGA scientist takes dark out of chicken meat http news.bbc.co.uk 1 hi education 4287712.stm BBC News Junk Food to be Banned in Schools Category Meat Category Fast food Category Meat industry de Formfleisch ... more details
Other uses P50 disambiguation In biochemistry , P sub 50 sub indicates the partial pressure of a gas required to achieve 50 enzyme saturation. ref http medical dictionary.thefreedictionary.com P 50 ref ref http www.lexingtonpulmonary.com education oxyhb oxyhb.html ref Values of P sub 50 sub are negatively correlated with substrate affinity, with lower values of P sub 50 sub corresponding to high affinity and vice versa . The term is analogous to the Michaelis Menten constant K sub m sub , which identifies the concentration of substrate required for an enzyme to achieve 50 of its maximum enzyme reaction rate reaction velocity . For example, the P sub 50 sub of myoglobin for oxygen O sub 2 sub is 130 pascal unit pascal s while the P sub 50 sub for hemoglobin adult hemoglobin is 3.5 kPa. Thus, when O sub 2 sub partial pressure is low, hemoglobin bound O sub 2 sub is more readily transferred to myoglobin. Myoglobin, found in high concentrations in muscle tissue, can then transfer the oxygen to muscle fiber s, where it will be used in the generation of energy to fuel muscle contraction. ref http www.ncbi.nlm.nih.gov pubmed 2706089 ref References Reflist DEFAULTSORT P50 Pressure Category Enzyme kinetics Category Units of pressure biochem stub fr P50 ... more details
Metmyoglobin is the oxidised form of the oxygen carrying protein myoglobin . Metmyoglobin is the cause of the characteristic brown colouration of meat that occurs as it ages. In living muscle , the concentration of metmyoglobin is vanishingly small, due to the presence of the enzyme metmyoglobin reductase , which, in the presence of the Cofactor biochemistry cofactor NADH and the coenzyme cytochrome b4 converts the Iron Fe sup 3 sup in the heme prosthetic group of metmyoglobin back to the Fe sup 2 sup of normal myoglobin. In meat, which is dead muscle , the normal processes of removing metmyoglobin are prevented from effecting this repair, or alternatively the rate of metmyoglobin formation exceeds their capacity, so that there is a net accumulation of metmyoglobin as the meat ages. External links MeshName Metmyoglobin Globins Category Hemoproteins chem stub de Metmyoglobin ja ... more details
Cleanup date October 2009 Chromoprotein A conjugated protein, such as hemoglobin, that contains a pigmented prosthetic group, such as hem in hemoglobin which makes blood red . Other examples of chromoprotein are myoglobin, cytochromes and flavoproteins. In hemoglobin chromoprotein tetramer MW 4 x 16.125 64.500 Hem Fe four pyrrol rings. Category Carotenoids Category Hemoproteins Category Pigments Category Proteins protein stub ca Cromoprote na mk pl Chromoproteiny ru uk zh ... more details
pigments. Respiration Physiology 57 201 211. ref MyoglobinMyoglobin is an oxygen transport protein used in muscles, but is also absent from all icefish skeletal muscles. In ten of the 16 species, myoglobin .... Variable expression of myoglobin among the hemoglobinless antarctic icefishes. Proceedings of the National Academy of Sciences of the United States of America 94 3420 3424. ref Myoglobin has been ... and myoglobin expression in antarctic icefishes. Journal of Experimental Biology 209 1791 1802. ref ... more details
Image Myoglobin 1mba.png thumb 300px An example of the globin fold, the oxygen carrying protein myoglobin PDB ID 1MBA from the mollusc Aplysia limacina . The globin fold is a common three dimensional tertiary structure fold in protein s. This fold typically consists of eight Verify source date October 2007 alpha helix alpha helices , although some proteins have additional helix extensions at their termini. The globin fold is found in its namesake proteins hemoglobin and myoglobin as well as in phycocyanin proteins. Because myoglobin was the first protein whose structure was solved, the globin fold was thus the first protein fold discovered. Since the globin fold contains only helices, it is classified as an all alpha protein fold . Helix packing The eight helices of the globin fold core share significant nonlocal structure, unlike other structural motif s in which amino acid s close to each other in primary sequence are also close in space. The helices pack together at an average angle of about 50 degrees, significantly steeper than other helical packings such as the helix bundle . The exact angle of helix packing depends on the sequence of the protein, because packing is mediated by the steric s and hydrophobic interactions of the amino acid side chain s near the helix interfaces. Sequence conservation Although the globin fold is highly evolution arily Conserved sequence conserved , the sequences that form the fold can have as low as 16 sequence identity. While the sequence specificity of the fold is not stringent, the hydrophobic core of the protein must be maintained and hydrophobic patches on the generally hydrophilic solvent exposed surface must be avoided in order for the structure to remain stable and soluble . The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule. This mutation creates a hydrophobic patch on the protein surface that promotes intermolecular aggregation, the molecular event that gives ... more details
Synzymes are substances with catalytic capabilities. The name synzyme is derived from synthetic enzyme . Current synzymes consist mainly of organic molecules tailored in such a way that they catalyse certain kinds of reactions. Like enzymes, they bind a transition state of a substrate in an acitve site, and like enzymes they generally obey Michaelis Menten kinetics . Derivatised proteins If Ru NH sub 3 sub sub 5 sub sup 3 sup is attached to certain histidine residues in a myoglobin protein, myoglobin is no longer a passive oxygen carrier, but gains enzmatic activity of an oxidase . Ascorbic acid is oxidised with molecular oxygen. Antibodies can act as enzymes, then named abzyme s, if they are selected against transition state analogues. Abzymes have a low K sub M sub , meaning that they readily bind a target molecule, but have low V sub max sub values, indicating a slow reaction rate. Synzymes from organic molecules Cyclodextrins are cap structures with a hydrophilic exterior but a hydrophobic interior. If pyridoxal is anchored in the interior the cyclodextran shows transaminase activity. See also Enzyme Abzyme Catalysis References Wiseman A. Designer enzyme and cell applications in industry and in environmental monitoring. J Chem Technol Biotechnol. 1993 56 1 3 13 Diekmann S. et al. Metal mediated reactions modeled after nature. J Biotechnol. 2002 Apr 90 2 73 94 External links http www.lsbu.ac.uk biology enztech artificial.html enzyme stub Category Enzymes ... more details
structure of myoglobin Image KendrewMyoglobin.jpg thumb 300px John Kendrew with model of myoglobin ... Biology in Cambridge . Kendrew determined the structure of the protein myoglobin , which ... embarked on the study of myoglobin , a molecule only a quarter the size of the hemoglobin molecule. His .... Whale myoglobin did give large crystals with clean X ray diffraction patterns. However, the problem ... whale myoglobin. Comparison between the amino acid sequences of sperm whale myoglobin and of human ... Structure and function in myoglobin and other proteins volume 18 issue 2, Part 1 pages 740 51 issn ... title A three dimensional model of the myoglobin molecule obtained by x ray analysis volume 181 ... title Orientation of the haem group in myoglobin and its relation to the polypeptide chain direction ... complexes of myoglobin and the position of the haem group volume 175 issue 4448 pages 206 7 issn 0028 ... last1 Kendrew first1 JC last2 Parrish last3 Marrack last4 Orlans title The species specificity of myoglobin ... more details
unreferenced date August 2009 Image Musclon2.jpg thumb 300px Muscle system The Sarcoplasm of a muscle fiber is comparable to the cytoplasm of other cells, but it houses unusually large amounts of glycosomes granules of stored glycogen and significant amounts of myoglobin , an oxygen binding protein. The calcium concentration in sarcoplasma is also a special element of the muscular fiber by means of which the contractions takes place and regulates. Other than the fact that it contains mostly myofibrils , its contents are otherwise comparable to those of the cytoplasm of other cells. It has a Golgi apparatus , near the Cell nucleus nucleus , mitochondria just on the inside of the cytoplasmic membrane or sarcolemma , as well as a smooth endoplasmic reticulum organized in an extensive network. External links eMedicineDictionary sarcoplasm http medical.merriam webster.com medical sarcoplasm Merriam Webster Dictionary http www.encyclopedia.com doc 1O8 sarcoplasm.html Sarcoplasm at Encyclopedia.com br br Muscle tissue Category Cell anatomy es Sarcoplasma io Sarkoplasmo nl Sarcoplasma ja pl Sarkoplazma pt Sarcoplasma ru vi C t ng ... more details
This is a table of permselectivity for different substances in the glomerulus of the kidney in renal filtration . class wikitable Substance Molecular mass ref name boron cite book author Walter F. Boron, Emile L. Boulpaep title Medical Physiology A Cellular And Molecular Approach publisher Elsevier Saunders location year pages isbn 1 4160 2328 3 oclc doi Page 761 ref Effective molecular radius Nanometre nm ref name boron Concentration conc. in ultrafiltrate BR conc. in blood plasma ref name boron sodium 23 0.1 1.0 potassium 39 0.14 1.0 chloride 35,5 0.18 1.0 water 18 0.15 1.0 urea 60 0.16 1.0 glucose 180 0.33 1.0 sucrose 342 0.44 1.0 polyethylene glycol 1.000 0.70 1.0 inulin 5.200 1.48 0.98 lysozyme 14.600 1.90 0.8 myoglobin 16.900 1.88 0.75 lactoglobulin 36.000 2.16 0.4 egg albumin 43.500 2.80 0.22 Bence Jones protein 44.000 2.77 1.0 hemoglobin 68.000 3.25 0.03 serum albumin 69.000 3.55 0.01 References references renal physiology category physiology ... more details
by dissection of Hoyle s argument made in relation to myoglobin . ref Evolution from Space 1982 ... different values at each position of v sup n sup possibilities. Therefore myoglobin, a protein ... must consider the smallest such space that contains a functional myoglobin. Neither n 153 nor v 20 can be accepted as minimal requirements, a priori. Myoglobin function is in fact a property of the folded ... myoglobin cannot be calculated. Reception Hoyle s Fallacy is rejected by all evolutionary ... more details
for long term use and contain a large amount of myoglobin , allowing the muscle to use oxygen more efficiently ... of the birds, are used for quick bursts of power which requires little of the meat darkening myoglobin ... more details
Infobox Disease Name PAGENAME Image Caption DiseasesDB 13135 ICD10 ICD10 T 79 5 t 79 ICD9 ICD9 958.5 ICDO OMIM MedlinePlus eMedicineSubj eMedicineTopic MeshID D003444 Crush syndrome also physical trauma traumatic rhabdomyolysis or Bywaters syndrome is a serious medical condition characterized by major Shock medical shock and renal failure after a crushing injury of skeletal muscle . Cases occur commonly in catastrophes such as earthquakes , such that victims have been trapped under fallen masonry. Pathophysiology The syndrome was discovered by United Kingdom British physician Eric Bywaters in patients during the 1941 London The Blitz Blitz . ref WhoNamedIt synd 3870 ref ref Bywaters EG, Beall D. Crush injuries with impairment of renal function . British Medical Journal Br Med J 1941 1 427 32 ref It is a reperfusion injury that appears after the release of the crushing pressure. The mechanism is believed to be the release into the bloodstream of muscle breakdown products notably myoglobin , potassium and phosphorus that are the products of rhabdomyolysis the breakdown of skeletal muscle damaged by ischemia ischemic conditions . The specific action on the kidney s is not understood completely, but may be due partly to nephrotoxicity nephrotoxic metabolite s of myoglobin. Seigo Minami , a Japanese physician, first reported the crush syndrome during 1923. ref Ueber Nierenveraenderungen nach Verschuettung. Seigo Minami, Virchows Arch. Patho. Anat. 1923, 245,247 67. ref ref Medical discoveries Who and when Schmidt JF. Springfield CC Thomas, 1959. p.115. ref ref Morton s medical bibliography An annotated check list of texts illustrating History of medicine Garrison Morton . Aldershot Solar Press 1911. p.654. ref Seigo Minami studied the pathology of 3 soldiers who died in World War I from insufficiency of the kidney. The renal changes were due to methohemoglobin infarction, resulting from the destruction of muscles, which is also seen in persons who are buried alive. The p ... more details
James P. Collman born 1932 in Beatrice, Nebraska is an American Professor of Chemistry. He is currently serving at Stanford University in California. Collman is considered a pioneer in bioinorganic and biomimetic chemistry. He developed a clearer understanding of the mechanisms of biological proteins, by studying synthetic analogs of biological systems which contain metal and metalloid atoms. His work on hemoglobin, myoglobin and cytochrome c oxidase allowed subsequent researchers to understand how the protein metal interactions allow these molecules to function. ref Chemical & Engineering News , 19 January 2009, p. 73 ref Career Collman received B.S. 1954 and M.S. degrees 1956 in Chemistry from the University of Nebraska Lincoln . He received a Ph.D. degree from the University of Illinois at Urbana Champaign in 1958 under Reynold C. Fuson . Upon receiving his Ph. D., Collman joined the faculty of University of North Carolina at Chapel Hill , remaining there until 1967, when he moved to Stanford University. He currently holds the George & Hilda M. Daubert Endowed Chair in Chemistry at Stanford. Collman has contributed to several aspects of transition metal chemistry. He has authored 3 books and over 366 Academic publishing scientific papers . In the 1960s his group demonstrated that certain metal acetylacetonate s undergo Friedel Crafts like reactions, indicating that these chelate rings have aromatic character. Through reviews as well as original research, his group popularized the oxidative addition reaction, leading to the discovery of new low valent complexes including Ru CO sub 3 sub PPh sub 3 sub sub 2 sub and IrCl N sub 2 sub PPh sub 3 sub sub 2 sub . Collman s reagent , Na sub 2 sub Fe CO sub 4 sub , prepared in his laboratories, enables certain C C coupling reactions in organic synthesis . He popularized the use of tetraphenylporphyrin as a Biomimicry biomimetic Ligand biochemistry ligand for exploring the structure and function of myoglobin , cytochrome P4 ... more details
Image Haem B 3D vdW.png thumb right 200px A space filling model model of Heme B cofactor. A hemeprotein or hemoprotein or haemoprotein , or heme protein , is a metalloprotein containing a heme prosthetic group , either Covalent bond covalently or noncovalently chemical bond bound to the protein itself. The iron in the heme is capable of undergoing oxidation and redox reduction usually to 2 and 3, though stabilized ferryl Fe sup 4 sup and even Fe sup 5 sup species are well known in the peroxidases . Hemoproteins probably evolved from a primordial strategy allowing to incorporate the iron Fe atom contained within the protoporphyrin IX ring of heme into proteins. This strategy has been maintained throughout evolution as it makes hemoproteins responsive to molecules that can bind divalent iron Fe . These molecules included, but are probably not restricted to, gaseous molecules, such as oxygen O sub 2 sub nitric oxide NO , carbon monoxide CO and hydrogen sulfide H sub 2 sub S . Once bound to the prosthetic heme groups of hemoproteins these gaseous molecules can modulate the activity function of those hemoproteins in a way that is said to afford signal transduction. Therefore, when produced in biologic systems cells , these gaseous molecules are referred to as gasotransmitters . Roles Hemoproteins have diverse biological functions including Oxygen transport hemoglobin myoglobin neuroglobin cytoglobin leghemoglobin Catalysis peroxidase s cytochrome c oxidase ligninase s Active transport Active membrane transport cytochrome s Electron transfer cytochrome c catalase Sensory FixL Oxygen sensor sGC Nitric Oxide sensor CooA CO sensor Defence vanabin External links MeshName Hemeproteins Category Hemoproteins protein stub Globins es Hemoprote na fr H moprot ine it Emoproteina ru sv Hemoprotein ... more details
. Myoglobin Mb low specificity for myocardial infarction 2 hours Myoglobin is used less than the other markers. Myoglobin is the primary oxygen carrying pigment of muscle tissue. It is high when muscle ... with a model combining myoglobin, creatine kinase MB, and clinical variables. TAMI 7 Study Group ... more details
Protoporphyrins are tetrapyrroles containing the following side chain s methyl 4 propionic acid 2 vinyl 2 Protoporphyrin IX is a biochemically widely used carrier molecule for divalent cations. Together with iron Fe 2 the body of the heme group of hemoglobin , myoglobin and many other heme containing enzymes like cytochrome c and catalase are formed. Complexed with magnesium ions Mg 2 the main part of the Chlorophylls are formed. Complexed with zinc ions Zn 2 it forms Zinc protoporphyrin . The number e.g. IX indicates the position of different side chains, but historically, as the nomenclature has grown, it has done so systematically only in parts. Protoporphyrin IX as a direct precursor of heme is accumulated by patients of erythropoietic protoporphyria , which is one of the genetic disorders of the biosynthesis of the heme pathway. It causes a severe photosensivity against visible light. The sensitivity of protoporphyrin IX against light is also used as a therapy against different forms of cancer photodynamic therapy , PDT . Protoporphyrins are deposited in the shells of the egg biology eggs of some bird s as a brown or red pigment, either as a ground colour or as spotting. This occurs in most passerine species, some ground nesting non passerines, such as wader s, gull s, nightjar s and sandgrouse , where it provides camouflage, and some brood parasite parasitic cuckoo s, which need to mimic their passerine hosts eggs. Protoporphyrins strengthen the egg shell, and are deposited where the shell is too thin as a result of calcium shortage. Spotting therefore tend to be heavier where the local soil is calcium deficient, and in the eggs laid last in a clutch. External links MeshName Protoporphyrins PubChem 4971 protoporphyrin IX Tetrapyrroles biochem stub Category Tetrapyrroles fr Protoporphyrine nl Protoporfyrine ja ... more details
Automatic taxobox binomial Borrelia anserina binomial authority Sakharoff 1891 Bergey et al. 1925 Borrelia anserina is a helical filiform spirochete bacteria with dimensions of approximately 8 20 0,2 0,3 Micrometre m and with about 5 to 8 spirals. Their mobility is very high. B. anserina can be colored with the May Grunwald Giemsa method . ref name Diurpaneu cite book author Gheorghe Rapunteanu, Sorin Rapunteanu editors title Bacteriologie Veterinara Speciala edition I publisher Editura AcademicPress, Cluj Napoca, Romania year 2005 id ISBN 973 7950 95 X ref Cultivation In Microbiological laboratories, B. anserina bacteria can be grown on special protein enriched mediums rich in ovoalbumins or animal tissue that contains Myoglobin , in wikt anaerobic anaerobic conditions. They can also be grown in embrionated chicken eggs. The laboratory cultivation of B. anserina is rarely done and constitutes a diagnostic method in bird borreliosis and spirochetosis. ref name Diurpaneu Pathogenity B. anserina is a pathogenic agent for birds chickens, turkeys, ducks etc. and causes a disease called borreliosis or spirochetosis . This bacteria is transmitted from bird to bird by ticks from the Argas and Ornitodorus genus. The major symptoms of an infection with B. anserina are anemia , diarrhea and severe neurological dysfunctions. Image Argastick.jpg thumb These two ticks represent the Argasidae soft ticks Lt , and the Ixodidae hard ticks References references External links http www.pubmedcentral.nih.gov articlerender.fcgi?artid 385494 A STUDY OF BORRELIA ANSERINA INFECTION SPIROCHETOSIS IN TURKEYS Category Poultry diseases veterinary med stub bacteria stub es Borrelia anserina fr Borrelia anserina ... more details
Irving Geis 18 October 1908 22 July 1997 was an United States American artist who worked closely with biologists . Geis s hand drawn work depicts many structures of biological macromolecules, such as DNA and protein s, including the first crystal structure of sperm whale myoglobin . He also served as a coauthor and illustrator of many biochemical books that were written by Albert Lehninger and Richard E. Dickerson , as well as the book How to Lie with Statistics by Darrell Huff . Geis was born in New York City , and lived in Anderson, South Carolina Anderson , South Carolina for a time. He studied architecture at Georgia Tech . References refbegin reflist cite journal last Dickerson first R. E. authorlink coauthors year 1997 month title Irving Geis, Molecular artist, 1908 1997 journal Protein Sci volume 6 issue pages 2483 2484 id url accessdate quote doi 10.1002 pro.5560061126 cite web url http www.hhmi.org news geis.html title HHMI Purchases Geis Archives accessdate 2008 02 29 work refend External links http www.sciam.com article.cfm?id a gallery for irving geis A Gallery for Irving Geis. by Kristin Leutwyler. Persondata Metadata see Wikipedia Persondata . NAME Geis, Irving ALTERNATIVE NAMES SHORT DESCRIPTION DATE OF BIRTH PLACE OF BIRTH DATE OF DEATH PLACE OF DEATH DEFAULTSORT Geis, Irving Category 1908 births Category 1997 deaths Category American illustrators Category Scientific illustrators Category Georgia Institute of Technology alumni US illustrator stub ... more details
saved book title Biochemistry subtitle An introduction cover image cover color Biochemistry An introduction This collection of Wikipedia articles is intended to supplement a standard textbook of biochemistry. Students may find its explanations complement their texts for greater clarity. In some areas its information will extend past their texts. In a few areas, information is still lacking but students are warmly welcomed to make up that deficit Cells and water Biochemistry Cell biology Cells Water Structural Biochemistry Nucleic acids Nucleic acid RNA DNA Proteins and amino acids Protein Amino acid Proteinogenic amino acid Properties of the twenty amino acids Myoglobin Hemoglobin Enzyme mechanisms Enzyme catalysis Enzyme kinetics Enzyme kinetics Lipids and membranes Lipid Biological membrane Membrane protein Cell membrane Carbohydrate structure Carbohydrate Polysaccharide Intermediary metabolism Metabolism Metabolism Overview of metabolism Carbohydrate metabolism Glycolysis Gluconeogenesis Glycogen Pentose phosphate pathway Citric acid cycle Citric acid cycle Oxidative phosphorylation Oxidative phosphorylation Photosynthesis Photosynthesis Lipid metabolism Fatty acid synthesis Lipogenesis Acetyl CoA carboxylase Fatty acid degradation Beta oxidation Nitrogen metabolism Nitrogen fixation Amino acid synthesis Nucleotide Urea cycle Integration of metabolism Hormone Signal transduction Diabetes mellitus Informational Macromolecules DNA synthesis and repair DNA replication DNA repair Oncogene Oncogenes RNA synthesis and processing Transcription genetics Transcription Regulation of gene expression Protein synthesis and modifications Translation genetics Translation Posttranslational modification Proteolysis Proteasome Category Wikipedia books on biology Biochemistry an introduction Category Wikipedia books on chemistry Biochemistry an introduction ... more details
Functional divergence is the process by which genes, after gene duplication , shift in function from an ancestral function. Functional divergence can result in either subfunctionalization , where a paralog specializes one of several ancestral functions, or neofunctionalization , where a totally new functional capability evolves. It is thought that this process of gene duplication and functional divergence is a major originator of molecular novelty and has produced the many large protein families that exist today ref Gu X. Functional divergence in protein family sequence evolution. Genetica. 2003 Jul 118 2 3 133 41. ref ref Fay JC, Wu CI. Sequence divergence, functional constraint, and selection in protein evolution. Annu Rev Genomics Hum Genet. 2003 4 213 35. ref . Many well known protein families are the result of this process, such as the ancient gene duplication event that led to the divergence of hemoglobin and myoglobin , the more recent duplication events that led to the various subunit expansions alpha and beta of vertebrate hemoglobin s ref Jay F. Storz, Federico G. Hoffmann, Juan C. Opazo, and Hideaki Moriyama. Adaptive Functional Divergence Among Triplicated Globin Genes in Rodents. Genetics. 2008 March 178 3 1623 1638. doi 10.1534 genetics.107.080903 ref , or the expansion of G protein alpha subunits ref Zheng Y, Xu D, Gu X. Functional divergence after gene duplication and sequence structure relationship a case study of G protein alpha subunits. J Exp Zool B Mol Dev Evol. 15 January 2007 308 1 85 96. ref References Reflist Refbegin Gu X. A simple statistical method for estimating type II cluster specific functional divergence of protein sequences. Mol Biol Evol. 2006 Oct 23 10 1937 45. Epub 24 July 2006. Refend DEFAULTSORT Functional Divergence Category Genetics Category Evolution Biology stub ... more details
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