Myoglobin is an iron- and oxygen-binding protein Proteins are organic compounds made of amino acids arranged in a linear chain and folded into a globular form. The amino acids in a polymer are joined together by the peptide bonds between the carboxyl and amino groups of adjacent amino acid residues. The sequence of amino acids in a protein is defined by the sequence of a gene, which is encoded found in the muscle tissue of vertebrates in general and in almost all mammals. It is related to hemoglobin, which is the iron- and oxygen-binding protein in blood, specifically in the red blood cells. The only time myoglobin is found in the bloodstream is when it is released following muscle injury. It is an abnormal finding, and can be diagnostically relevant when found in blood. [2]

Myoglobin (abbreviated Mb) is a single-chain In biochemistry and chemistry, the tertiary structure of a protein or any other macromolecule is its three-dimensional structure, as defined by the atomic coordinates globular protein of 153[3] or 154[4] amino acids Amino acids are molecules containing an amine group, a carboxylic acid group and a side chain that varies between different amino acids. These molecules contain the key elements of carbon, hydrogen, oxygen, and nitrogen. These molecules are particularly important in biochemistry, where this term refers to alpha-amino acids with the general formula, containing a heme A heme or haem (British English) is a prosthetic group that consists of an iron atom contained in the center of a large heterocyclic organic ring called a porphyrin. Not all porphyrins contain iron, but a substantial fraction of porphyrin-containing metalloproteins have heme as their prosthetic group; these are known as hemoproteins. Hemes are (iron Iron is the most common element in the earth as a whole, and the fourth most common in the Earth's crust. It is produced as a result of stellar fusion in high-mass stars, and it is the heaviest stable element produced by stellar fusion because the fusion of iron is the last nuclear fusion reaction that is exothermic. Iron is the most widely used-containing porphyrin Porphyrins are a group of organic compounds of which many occur in nature, most well-known as the pigment in red blood cells. They are heterocyclic macrocycles characterised by the presence of four modified pyrrole subunits interconnected at their α carbon atoms via methine bridges . Porphyrins are aromatic, and they obey Hückel's rule for) prosthetic group A cofactor is a non-protein chemical compound that is bound to a protein and is required for the protein's biological activity. These proteins are commonly enzymes and cofactors can be considered "helper molecules" that assist in biochemical transformations. Cofactors can also be classified depending on how tightly they bind to an enzyme, in the center around which the remaining apoprotein folds. It has eight alpha helices and a hydrophobic core. It has a molecular weight of 16,700 daltons The unified atomic mass unit or atomic mass unit , or dalton (Da) or, sometimes, universal mass unit (u), is a unit of mass used to express atomic and molecular masses. It is the approximate mass of a hydrogen atom, a proton, or a neutron, and is the primary oxygen Oxygen (pronounced /ˈɒksɨdʒɨn/, OK-si-jin, from the Greek roots ὀξύς (acid, literally "sharp", from the taste of acids) and -γενής (-genēs) (producer, literally begetter), is the element with atomic number 8 and represented by the symbol O. It is a member of the chalcogen group on the periodic table, and is a highly-carrying pigment Biological pigments, also known simply as pigments or biochromes[citation needed] are substances produced by living organisms that have a color resulting from selective color absorption. Biological pigments include plant pigments and flower pigments. Many biological structures, such as skin, eyes, fur and hair contain pigments such as melanin in of muscle Muscle is the contractile tissue of animals and is derived from the mesodermal layer of embryonic germ cells. Muscle cells contain contractile filaments that move past each other and change the size of the cell. They are classified as skeletal, cardiac, or smooth muscles. Their function is to produce force and cause motion. Muscles can cause tissues.[4] Unlike the blood-borne hemoglobin Hemoglobin is the iron-containing oxygen-transport metalloprotein in the red blood cells of vertebrates, and the tissues of some invertebrates. Hemoglobin in the blood is what transports oxygen from the lungs or gills to the rest of the body (i.e. the tissues) where it releases the oxygen for cell use, to which it is structurally related,[5] this protein does not exhibit cooperative binding In biochemistry, a macromolecule exhibits cooperative binding if its affinity for its ligand changes with the amount of ligand already bound of oxygen, since positive cooperativity is a property of multimeric/oligomeric In chemistry, an oligomer consists of a few monomer units , in contrast to a polymer that, at least in principle, consists of an unlimited number of monomers. Dimers, trimers and tetramers are oligomers. Many oils are oligomeric, such as liquid paraffin. Plasticizers are oligomeric esters widely used to soften thermoplastics such as PVC. They may proteins only. 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 Dissociation in chemistry and biochemistry is a general process in which ionic compounds separate or split into smaller particles, ions, or radicals, usually in a reversible manner. When a Bronsted-Lowry acid is put in water, a covalent bond between an electronegative atom and a hydrogen atom is broken by heterolytic fission, which gives a proton curve. High concentrations of myoglobin in muscle cells allow organisms to hold their breaths longer. Diving mammals such as whales and seals have muscles with particularly high myoglobin abundance.[6]

Myoglobin was the first protein to have its three-dimensional structure revealed.[7] In 1958, John Kendrew Sir John Cowdery Kendrew, CBE, FRS was an English biochemist and crystallographer who shared the 1962 Nobel Prize in Chemistry with Max Perutz; their group in the Cavendish Laboratory investigated the structure of heme-containing proteins and associates successfully determined the structure of myoglobin by high-resolution X-ray crystallography X-ray crystallography is a method of determining the arrangement of atoms within a crystal, in which a beam of X-rays strikes a crystal and diffracts into many specific directions. From the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal.[8] For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry The Nobel Prize in Chemistry is awarded annually by the Royal Swedish Academy of Sciences to scientists in the various fields of chemistry. It is one of the five Nobel Prizes established by the will of Alfred Nobel in 1895, awarded for outstanding contributions in chemistry, physics, literature, peace, and physiology or medicine. This award is with Max Perutz Max Ferdinand Perutz, OM, CBE was an Austrian-born British molecular biologist, who was awarded the Nobel Prize for Chemistry in 1962, shared with John Kendrew for their studies of the structures of hemoglobin and globular proteins. At Cambridge he supervised the PhD work of Francis Crick and James Watson in the Cavendish Laboratory as they.[9] Despite being one of the most studied proteins in biology, its true physiological function is not yet conclusively established: mice genetically engineered to lack myoglobin are viable, but showed a 30% reduction in cardiac systolic output. They adapted to this deficiency through hypoxic genetic mechanisms and increased vasodilation.[10] In humans myoglobin is encoded by the MB gene A gene is a unit of heredity in a living organism. It is normally a stretch of DNA that codes for a type of protein or for an RNA chain that has a function in the organism. All living things depend on genes, as they specify all proteins and functional RNA chains. Genes hold the information to build and maintain an organism's cells and pass genetic.[11]

Contents

Meat colour

An X-ray diffraction X-ray scattering techniques are a family of non-destructive analytical techniques which reveal information about the crystallographic structure, chemical composition, and physical properties of materials and thin films. These techniques are based on observing the scattered intensity of an X-ray beam hitting a sample as a function of incident and image for the protein myoglobin

Myoglobin forms pigments A pigment is a material that changes the color of reflected or transmitted light as the result of wavelength-selective absorption. This physical process differs from fluorescence, phosphorescence, and other forms of luminescence, in which a material emits light responsible for making meat red Red meat in traditional culinary terminology is meat which is red when raw and not white when cooked. Red meat includes the meat of most adult mammals and some fowl . In the nutritional sciences, red meat includes all mammal meat. The color that meat takes is partly determined by the charge of the iron atom in myoglobin and the oxygen attached to it. When meat is in its raw state, the iron atom is in the +2 oxidation state, and is bound to a dioxygen molecule (O2). Meat cooked well done is brown because the iron atom is now in the +3 oxidation state, having lost an electron, and is now coordinated by a water molecule. Under some conditions, meat can also remain pink all through cooking, despite being heated to high temperatures. If meat has been exposed to nitrites The nitrite ion is NO2−. The anion is bent, being isoelectronic with ozone. More generally, a nitrite compound is either a salt or an ester of nitrous acid, it will remain pink because the iron atom is bound to NO, nitric oxide Nitric oxide or nitrogen monoxide (systematic name) is a chemical compound with chemical formula N (true of, e.g., corned beef Corned beef is a particular style of brine-cured beef. The "corn" in corned beef refers to the "corns" or grains of coarse salts used to cure it. The Oxford English Dictionary dates the usage of corn, meaning "small hard particle, a grain, as of sand or salt." Potassium nitrate is often added to the brine to help or cured hams Ham is the thigh and rump of pork from the haunch of a pig or boar. Although it may be cooked and served fresh, most ham is cured in some fashion. Cuts referred to as ham in the U.S. are also called gammon in the U.K., South Africa, Isle of Man, and Ireland). Grilled meats can also take on a pink "smoke ring" that comes from the iron binding a molecule of carbon monoxide to give metmyoglobin.[12] Raw meat packed in a carbon monoxide atmosphere also shows this same pink "smoke ring" due to the same coordination chemistry. Notably, the surface of the raw meat also displays the pink color, which is usually associated in consumers' minds with fresh meat. This artificially-induced pink color can persist in the meat for a very long time, reportedly up to one year. [13] Hormel and Cargill are both reported to use this meat-packing process, and meat treated this way has been in the consumer market since 2003.[14] 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 from damaged muscle tissue (rhabdomyolysis Rhabdomyolysis is the rapid breakdown of skeletal muscle (rhabdomyo) due to injury to muscle tissue. The muscle damage may be caused by physical (e.g., crush injury), chemical, or biological factors. The destruction of the muscle leads to the release of the breakdown products of damaged muscle cells into the bloodstream; some of these, such as), which has very high concentrations of myoglobin. The released myoglobin is filtered by the kidneys The kidneys are paired organs with several functions. They are seen in many types of animals, including vertebrates and some invertebrates. They are an essential part of the urinary system and also serve homeostatic functions such as the regulation of electrolytes, maintenance of acid-base balance, and regulation of blood pressure. They serve the but is toxic to the renal tubular epithelium and so may cause acute renal failure Acute kidney injury , previously called acute renal failure (ARF), is a rapid loss of kidney function. Its causes are numerous and include low blood volume, exposure to toxins, and prostate enlargement. AKI is diagnosed on the basis of clinical history, such as decreased urine production, and characteristic laboratory findings, such as elevated.[15]

Myoglobin is a sensitive marker for muscle injury, making it a potential marker for heart attack Myocardial infarction or acute myocardial infarction (AMI), commonly known as a heart attack, is the interruption of blood supply to part of the heart, causing heart cells to die. This is most commonly due to occlusion (blockage) of a coronary artery following the rupture of a vulnerable atherosclerotic plaque, which is an unstable collection of in patients with chest pain Chest pain may be a symptom of a number of serious conditions and is generally considered a medical emergency. Even though it may be determined that the pain is non-cardiac in origin, this is often a diagnosis of exclusion made after ruling out more serious causes of the pain.[16] However, elevated myoglobin has low specificity for acute myocardial infarction (AMI) Myocardial infarction or acute myocardial infarction (AMI), commonly known as a heart attack, is the interruption of blood supply to part of the heart, causing heart cells to die. This is most commonly due to occlusion (blockage) of a coronary artery following the rupture of a vulnerable atherosclerotic plaque, which is an unstable collection of and thus CK-MB Creatine kinase , also known as creatine phosphokinase (CPK) or phospho-creatine kinase (and sometimes wrongly as creatinine kinase), is an enzyme (EC 2.7.3.2) expressed by various tissues and cell types. CK catalyses the conversion of creatine and consumes adenosine triphosphate (ATP) to create phosphocreatine and adenosine diphosphate (ADP), cTnT Troponin is a complex of three regulatory proteins that is integral to muscle contraction in skeletal and cardiac muscle, but not smooth muscle, ECG Electrocardiography is a transthoracic interpretation of the electrical activity of the heart over time captured and externally recorded by skin electrodes. It is a noninvasive recording produced by an electrocardiographic device. The etymology of the word is derived from the Greek electro, because it is related to electrical activity, cardio,, and clinical signs should be of course be taken into account to make the diagnosis.

Structure and bonding

Myoglobin contains a porphyrin Porphyrins are a group of organic compounds of which many occur in nature, most well-known as the pigment in red blood cells. They are heterocyclic macrocycles characterised by the presence of four modified pyrrole subunits interconnected at their α carbon atoms via methine bridges . Porphyrins are aromatic, and they obey Hückel's rule for ring with an iron center. There is a proximal histidine Histidine is one of the 22 proteinogenic amino acids. In terms of nutrition, histidine is considered an essential amino acid in human infants. After reaching several years of age, humans begin to synthesize it, at which point it becomes a non-essential amino acid. Its codons are CAU and CAC group attached directly to the iron center, and a distal histidine group on the opposite face, not bonded to the iron.

Many functional models of myoglobin have been studied. One of the most important is that of picket fence porphyrin by James Collman. This model was used to show the importance of the distal prosthetic group A cofactor is a non-protein chemical compound that is bound to a protein and is required for the protein's biological activity. These proteins are commonly enzymes and cofactors can be considered "helper molecules" that assist in biochemical transformations. Cofactors can also be classified depending on how tightly they bind to an enzyme,. It serves three functions:

  1. To form hydrogen bonds A hydrogen bond is the attractive interaction of a hydrogen atom with an electronegative atom, like nitrogen, oxygen or fluorine . The hydrogen must be covalently bonded to another electronegative atom to create the bond. These bonds can occur between molecules (intermolecularly), or within different parts of a single molecule (intramolecularly) with the dioxygen Oxygen (pronounced /ˈɒksɨdʒɨn/, OK-si-jin, from the Greek roots ὀξύς (acid, literally "sharp", from the taste of acids) and -γενής (-genēs) (producer, literally begetter), is the element with atomic number 8 and represented by the symbol O. It is a member of the chalcogen group on the periodic table, and is a highly moiety In organic chemistry, functional groups are specific groups of atoms within molecules that are responsible for the characteristic chemical reactions of those molecules. The same functional group will undergo the same or similar chemical reaction regardless of the size of the molecule it is a part of. However, its relative reactivity can be, increasing the O2 binding constant
  2. To prevent the binding of carbon monoxide Carbon monoxide , also called carbonic oxide, is a colorless, odorless and tasteless gas which is slightly lighter (M = 28.0) than air (M = 28.8). It is highly toxic to humans and animals in higher quantities, although it is also produced in normal animal metabolism in low quantities, and is thought to have some normal biological functions, whether from within or without the body. Carbon monoxide binds to iron in an end-on fashion, and is hindered by the presence of the distal histidine Histidine is one of the 22 proteinogenic amino acids. In terms of nutrition, histidine is considered an essential amino acid in human infants. After reaching several years of age, humans begin to synthesize it, at which point it becomes a non-essential amino acid. Its codons are CAU and CAC, which forces it into a bent conformation. CO binds to heme 23,000 times better than O2, but only 200 times better in hemoglobin Hemoglobin is the iron-containing oxygen-transport metalloprotein in the red blood cells of vertebrates, and the tissues of some invertebrates. Hemoglobin in the blood is what transports oxygen from the lungs or gills to the rest of the body (i.e. the tissues) where it releases the oxygen for cell use and myoglobin. Oxygen binds in a bent fashion, which can fit with the distal histidine.[17]
  3. To prevent irreversible dimerization A dimer is a chemical or biological entity consisting of two structurally similar subunits called monomers, which are joined by bonds, which can be strong or weak of the oxymyoglobin with another deoxymyoglobin species

See also

References

  1. ^ PDB The Protein Data Bank is a repository for the 3-D structural data of large biological molecules, such as proteins and nucleic acids. (See also crystallographic database). The data, typically obtained by X-ray crystallography or NMR spectroscopy and submitted by biologists and biochemists from around the world, can be accessed at no charge on the 1MBO; Takano T (March 1977). "Structure of myoglobin refined at 2.0 Å resolution. II. Structure of deoxymyoglobin from sperm whale". J. Mol. Biol. 110 (3): 569–84. doi A digital object identifier is a character string used to uniquely identify an electronic document or other object. Metadata about the object is stored in association with the DOI name and this metadata may include a location, such as a URL, where the object can be found. The DOI for a document is permanent, whereas its location and other metadata:10.1016/S0022-2836(77)80112-5. PMID A PMID is a unique number assigned to each PubMed citation of life sciences and biomedical scientific journal articles. The related Pubmed Central archive may additionally assign a separate number, a PMCID (PubMed Central Identifier), normally written with a PMC prefix 845960.
  2. ^ Nelson, D. L.; Cox, M. M. (2000). Lehninger Principles of Biochemistry, 3rd ed. New York, NY: Worth Publishers, p 206
  3. ^ Hendgen-Cotta, U.; Kelm, M.; Rassaf, T. (2009). "A highlight of myoglobin diversity: the nitrite reductase activity during myocardial ischemia-reperfusion". Nitric oxide : biology and chemistry / official journal of the Nitric Oxide Society 22 (2): 75. doi:10.1016/j.niox.2009.10.003. PMID 19836457.
  4. ^ a b George A. Ordway and Daniel J. Garry (2004). "Myoglobin: an essential hemoprotein in striated muscle". Journal of Experimental Biology 207 (Pt 20): 3441–3446. doi:10.1242/jeb.01172. PMID 15339940.
  5. ^ Harvey Lodish, Arnold Berk, Lawrence S. Zipursky, Paul Matsudaira, David Baltimore and James Darnell (2000). "Evolutionary tree showing the globin protein family members myoglobin and hemoglobin". Molecular Cell Biology (Fourth ed.). W. H. FREEMAN. ISBN 0-7167-3136-3. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Search&db=books&doptcmdl=GenBookHL&term=myoglobin+AND+mcb%5Bbook%5D+AND+105134%5Buid%5D&rid=mcb.figgrp.540.
  6. ^ Nelson, D. L.; Cox, M. M. (2000). Lehninger Principles of Biochemistry, 3rd ed. New York, NY: Worth Publishers, p 206
  7. ^ (U.S.) National Science Foundation: Protein Data Bank Chronology (Jan. 21, 2004). Retrieved 3.17.2010
  8. ^ JC Kendrew, G Bodo, HM Dintzis, RG Parrish, H Wyckoff, and DC Phillips (1958). "A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis". Nature 181 (4610): 662–666. doi:10.1038/181662a0. PMID 13517261.
  9. ^ The Nobel Prize in Chemistry 1962
  10. ^ Mammen PP, Kanatous SB, Yuhanna IS, Shaul PW, Garry MG, Balaban RS, Garry DJ (2003). "Hypoxia-induced left ventricular dysfunction in myoglobin-deficient mice". American Journal of Physiology. Heart and Circulatory Physiology 285(5) (5): H2132–41. doi:10.1152/ajpheart.00147.2003. PMID 12881221.
  11. ^ Akaboshi E (1985). "Cloning of the human myoglobin gene". Gene 33 (3): 241–9. doi:10.1016/0378-1119(85)90231-8. PMID 2989088.
  12. ^ McGee, H: "On Food and Cooking: The Science and Lore of the Kitchen, page 148. Scribner: New York, 2004. ISBN 0-684-80001-2
  13. ^ Minneapolis Star Tribune, Nov. 14, 2007 http://www.startribune.com/10223/story/1548852.html
  14. ^ Minneapolis Star Tribune, October 31, 2007 http://www.startribune.com/535/story/1518775.html
  15. ^ Toshio Naka, Daryl Jones, Ian Baldwin, Nigel Fealy, Samantha Bates, Hermann Goehl, Stanislao Morgera, Hans H. Neumayer and Rinaldo Bellomo (2005). "Myoglobin clearance by super high-flux hemofiltration in a case of severe rhabdomyolysis: a case report". Critical Care 9 (2): R90–R95. doi:10.1186/cc3034. PMID 15774055.
  16. ^ M. Weber, M. Rau, K. Madlener, A. Elsaesser, D. Bankovic, V. Mitrovic and C. Hamm (2005). "Diagnostic utility of new immunoassays for the cardiac markers cTnI, myoglobin and CK-MB mass". Clinical Biochemistry 38 (11): 1027. doi:10.1016/j.clinbiochem.2005.07.011. PMID 16125162.
  17. ^ J. P. Collman, J. I. Brauman, T. R. Halbert, and K. S. Suslick (1976). "Nature of Oxygen and Carbon Monoxide Binding to Metalloporphyrins and Heme Proteins". Proceedings of the National Academy of Sciences of the United States of America 73 (10): 3333–3337. doi:10.1073/pnas.73.10.3333. PMID 1068445. PMC 431107. http://www.pnas.org/cgi/content/abstract/73/10/3333.

Further reading

External links

Proteins: hemeproteins
Globins
Hemoglobin
Subunits

Alpha locus on 16: α (HBA1, HBA2) · ζ (HBZ) · θ (HBQ1) · μ (HBM)

Beta locus on 11: β (HBB) · δ (HBD) · γ (HBG1, HBG2) · ε (HBE1)
Tetramers

stages of development: HbA (α2β2) · HbA2 (α2δ2) · HbF/Fetal (α2γ2) · HbE Gower 2 (α2ε2) · HbE Gower 1 (ζ2ε2)

pathology: HbH (β4) · Barts (γ4) · HbS (α2βS2) · HbC (α2βC2) · HbE (α2βE2)
Compounds Carboxyhemoglobin · Carbaminohemoglobin · Oxyhemoglobin/Deoxyhemoglobin · Sulfhemoglobin
Other human Glycosylated hemoglobin · Methemoglobin
Nonhuman Chlorocruorin · Erythrocruorin
Other

human: Myoglobin (Metmyoglobin) · Neuroglobin · Cytoglobin

plant: Leghemoglobin
Other Cytochrome (Cytochrome b, Cytochrome P450) · Hemocyanin · Methemalbumin

: MYL

/ (, , )

//, /,

drug (//),

Medical test: Serology, reference range: Clinical biochemistry blood tests (including BMP, CMP)
Fluid/electrolytes

electrolytes (Na+/K+, Cl-/HCO3-) · renal function, BUN-to-creatinine ratio (BUN/Creatinine) · Ca

derived values: Plasma osmolality · Serum osmolal gap
Acid-base homeostasis Arterial blood gas · Base excess · Anion gap · CO2 content
Nutrition: Iron tests

Transferrin saturation = Serum iron / Total iron-binding capacity

Ferritin · Transferrin · Transferrin receptor
Endocrine

ACTH stimulation test · Thyroid function tests (TSH)

Blood sugar: Glucose test · C-peptide · Fructosamine · Glycated hemoglobin
Metabolic Blood lipids
Cardiac marker Troponin test · CPK-MB test · LDH · Myoglobin · Glycogen phosphorylase isoenzyme BB
Liver function tests protein tests (Human serum albumin, Serum total protein) · ALP · transaminases (ALT, AST, AST/ALT ratio) · Bilirubin (Unconjugated, Conjugated)

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, drug (), ,

PDB Gallery
1m6c: V68N MYOGLOBIN WITH CO
1m6m: V68N MET MYOGLOBIN
1mdn: WILD TYPE MYOGLOBIN WITH CO
1mnh: INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS: ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN
1mni: ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN. BIS-IMIDAZOLE LIGATION IN THE HIS64-->VAL(SLASH)VAL68-->HIS DOUBLE MUTANT
1mnj: INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS: ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN
1mnk: INTERACTIONS AMONG RESIDUES CD3, E7, E10 AND E11 IN MYOGLOBINS: ATTEMPTS TO SIMULATE THE O2 AND CO BINDING PROPERTIES OF APLYSIA MYOGLOBIN
1mno: V68N MYOGLOBIN OXY FORM
1mwc: WILD TYPE MYOGLOBIN WITH CO
1mwd: WILD TYPE DEOXY MYOGLOBIN
1myg: HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB(LYS45-> ARG) AND MB(LYS45-> SER)
1myh: HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB(LYS45-> ARG) AND MB(LYS45-> SER)
1myi: HIGH RESOLUTION X-RAY STRUCTURES OF PIG METMYOGLOBIN AND TWO CD3 MUTANTS MB(LYS45-> ARG) AND MB(LYS45-> SER)
1myj: DISTAL POLARITY IN LIGAND BINDING TO MYOGLOBIN: STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF A THREONINE68(E11) MUTANT
1pmb: THE DETERMINATION OF THE CRYSTAL STRUCTURE OF RECOMBINANT PIG MYOGLOBIN BY MOLECULAR REPLACEMENT AND ITS REFINEMENT
1yca: DISTAL POCKET POLARITY IN LIGAND BINDING TO MYOGLOBIN: DEOXY AND CARBONMONOXY FORMS OF A THREONINE68 (E11) MUTANT INVESTIGATED BY X-RAY CRYSTALLOGRAPHY AND INFRARED SPECTROSCOPY
1ycb: DISTAL POCKET POLARITY IN LIGAND BINDING TO MYOGLOBIN: DEOXY AND CARBONMONOXY FORMS OF A THREONINE68 (E11) MUTANT INVESTIGATED BY X-RAY CRYSTALLOGRAPHY AND INFRARED SPECTROSCOPY
2mm1: X-RAY CRYSTAL STRUCTURE OF A RECOMBINANT HUMAN MYOGLOBIN MUTANT AT 2.8 ANGSTROMS RESOLUTION

Categories: Human proteins | Hemoproteins

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Dolphin . myoglobin. protein is used as an example to show how EMBL can be used to locate bioinformatics data on a protein of interest. tutorial bioinformatics embl protein data fasta sequence.

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'Myoglobin' Answers
The protein chains in myoglobin and haemoglobin provide the haem groups with hydrophobic?
Q. The protein chains in myoglobin and haemoglobin provide the haem groups with hydrophobic environments. Why is this important?
Asked by M-Z - Tue Jun 2 16:35:55 2009 - - 1 Answers - 0 Comments

A. Binding of haem to the protein (haemoglobin or myoglobin) is augmented by hydrophobic bonding (the haem lies in a hydrophobic pocket of the folded polypeptide chain) and by salt bridges between acidic and basic amino acids of the protein.
Answered by Asha - Sat Jun 6 01:13:25 2009

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