Myoglobinuria historical perspective: Difference between revisions
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Myoglobin was the first protein to have its three-dimensional structure revealed by [[X-ray crystallography]].<ref>[https://www.nsf.gov/news/news_summ.jsp?cntn_id=100689 (U.S.) National Science Foundation: Protein Data Bank Chronology (Jan. 21, 2004)]. Retrieved 3.17.2010</ref> | ==Discovery== | ||
* In 1958 [[John Kendrew]] and associates announced that they have discovered that [[Myoglobin]] was the first protein to have its three-dimensional structure revealed by [[X-ray crystallography]].<ref>[https://www.nsf.gov/news/news_summ.jsp?cntn_id=100689 (U.S.) National Science Foundation: Protein Data Bank Chronology (Jan. 21, 2004)]. Retrieved 3.17.2010</ref> .<ref name="architecture">{{cite journal | vauthors = Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff H, Phillips DC | title = A three-dimensional model of the myoglobin molecule obtained by x-ray analysis | journal = Nature | volume = 181 | issue = 4610 | pages = 662–6 | date = Mar 1958 | pmid = 13517261 | doi = 10.1038/181662a0 | bibcode = 1958Natur.181..662K }}</ref> | |||
* For this discovery, John Kendrew shared the 1962 [[Nobel Prize in chemistry]] with [[Max Perutz]].<ref name="nobel">[http://nobelprize.org/chemistry/laureates/1962/index.html The Nobel Prize in Chemistry 1962]</ref> | |||
==Landmark Events in the Development of Treatment Strategies== | |||
* Despite being one of the most studied proteins in biology, its physiological function is not yet conclusively established: mice genetically engineered to lack myoglobin can be viable and fertile but show many cellular and physiological adaptations to overcome the loss. Through observing these changes in myoglobin-deplete mice, it is hypothesised that myoglobin function relates to increased oxygen transport to muscle, oxygen storage and as a scavenger of [[reactive oxygen species]].<ref name="mice-function">{{cite journal | vauthors = Garry DJ, Kanatous SB, Mammen PP | title = Molecular insights into the functional role of myoglobin | journal = Advances in Experimental Medicine and Biology | volume = 618 | pages = 181-93 | date = 2007 | pmid = 18269197 | doi = 10.1007/978-0-387-75434-5_14 }}</ref> | |||
==References== | ==References== | ||
Latest revision as of 12:37, 10 September 2018
Discovery
- In 1958 John Kendrew and associates announced that they have discovered that Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystallography.[1] .[2]
- For this discovery, John Kendrew shared the 1962 Nobel Prize in chemistry with Max Perutz.[3]
Landmark Events in the Development of Treatment Strategies
- Despite being one of the most studied proteins in biology, its physiological function is not yet conclusively established: mice genetically engineered to lack myoglobin can be viable and fertile but show many cellular and physiological adaptations to overcome the loss. Through observing these changes in myoglobin-deplete mice, it is hypothesised that myoglobin function relates to increased oxygen transport to muscle, oxygen storage and as a scavenger of reactive oxygen species.[4]
References
- ↑ (U.S.) National Science Foundation: Protein Data Bank Chronology (Jan. 21, 2004). Retrieved 3.17.2010
- ↑ Kendrew JC, Bodo G, Dintzis HM, Parrish RG, Wyckoff H, Phillips DC (Mar 1958). "A three-dimensional model of the myoglobin molecule obtained by x-ray analysis". Nature. 181 (4610): 662–6. Bibcode:1958Natur.181..662K. doi:10.1038/181662a0. PMID 13517261.
- ↑ The Nobel Prize in Chemistry 1962
- ↑ Garry DJ, Kanatous SB, Mammen PP (2007). "Molecular insights into the functional role of myoglobin". Advances in Experimental Medicine and Biology. 618: 181–93. doi:10.1007/978-0-387-75434-5_14. PMID 18269197.