Sandbox Reserved 303

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=Thermolysin=
=Thermolysin=
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Thermolysin is a protein that is isolated from the thermophile ''Bacillus thermoproteolyticus"". <ref>Matthews. (1988).</ref> This protein is characterized by a remarkable stability under heat and protein denaturants. <ref>Vita et al., (1985).</ref> The structure does not contain any stabilizing disulfide bonds.<ref>Fontana et al., (1977).</ref> Instead, Thermolysin binds four calcium ions that are necessary for its thermal stability. <ref>Matthews. (1988).</ref>
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Thermolysin is a protein that is isolated from the thermophile ''Bacillus thermoproteolyticus''. <ref>Matthews. (1988).</ref> This protein is characterized by a remarkable stability under heat and protein denaturants. <ref>Vita et al., (1985).</ref> The structure does not contain any stabilizing disulfide bonds.<ref>Fontana et al., (1977).</ref> Instead, Thermolysin binds four calcium ions that are necessary for its thermal stability. <ref>Matthews. (1988).</ref>
[http://ellen.warnerbros.com/ Ellen]
[http://ellen.warnerbros.com/ Ellen]

Revision as of 06:41, 12 March 2011

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.
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Thermolysin

Thermolysin is a protein that is isolated from the thermophile Bacillus thermoproteolyticus. [1] This protein is characterized by a remarkable stability under heat and protein denaturants. [2] The structure does not contain any stabilizing disulfide bonds.[3] Instead, Thermolysin binds four calcium ions that are necessary for its thermal stability. [4] Ellen


PDB ID 1q8k

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1q8k, 15 NMR models ()
Gene: EIF2S1 OR EIF2A (Homo sapiens)
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Works Cited

  1. ↑ Matthews. (1988).
  2. ↑ Vita et al., (1985).
  3. ↑ Fontana et al., (1977).
  4. ↑ Matthews. (1988).
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