Sandbox Reserved 1228 - Revision history

Danelle Hale at 15:17, 2 May 2017

Danelle Hale — Tue, 02 May 2017 15:17:36 GMT

←Older revision		Revision as of 15:17, 2 May 2017
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	== Structure ==		== Structure ==
-	<span> Ectatomin is a dimeric peptide. Both subunits, A and B, are formed by two alpha-helixes and four residues forming a hinge region which all combine to form a hairpin structure. The two subunits are then connected by a disulfide bond. All of this combines to form a four alpha-helical bundle structure in aqueous solution. The toxin has a molecular weight of 7,928 Da. [2]	+	<span> Ectatomin is a dimeric peptide. Both subunits, A and B, are formed by two alpha-helixes and four residues forming a hinge region which all combine to form a hairpin structure. The two subunits are then connected by a disulfide bond. All of this combines to form a four alpha-helical bundle structure in aqueous solution. [3] The toxin has a molecular weight of 7,928 Da. [2]

	== Subunits ==		== Subunits ==

Danelle Hale at 14:54, 2 May 2017

Danelle Hale — Tue, 02 May 2017 14:54:30 GMT

←Older revision		Revision as of 14:54, 2 May 2017
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	== ECTATOMIN 1ECI ==		== ECTATOMIN 1ECI ==
	<StructureSection load='1eci' size='340' side='right' caption='Ectatomin'</scene>		<StructureSection load='1eci' size='340' side='right' caption='Ectatomin'</scene>
-	Ectatomin (Ea) is a water soluble toxic component from <i> Ectatomma tuberculatum </i> ant venom. It contains two homologous polypeptide chains with 37 and 34 residues, respectively. The chains are linked together by a disulfide bond.[1] Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims. [4] Ectatomin is responsible for about 90% of the total toxicity of the venom produced by the ants. [5]	+	Ectatomin (Ea) is a water soluble toxic component from <i> Ectatomma tuberculatum </i> ant venom. It contains two homologous polypeptide chains with 37 and 34 residues, respectively. The chains are linked together by a disulfide bond.[1] Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims. [5] Ectatomin is responsible for about 90% of the total toxicity of the venom produced by the ants. [2]



	== Structure ==		== Structure ==
-	<span> Ectatomin is a dimeric peptide. Both subunits, A and B, are formed by two alpha-helixes and four residues forming a hinge region which all combine to form a hairpin structure. The two subunits are then connected by a disulfide bond. All of this combines to form a four alpha-helical bundle structure in aqueous solution. The toxin has a molecular weight of 7,928 Da. [5]	+	<span> Ectatomin is a dimeric peptide. Both subunits, A and B, are formed by two alpha-helixes and four residues forming a hinge region which all combine to form a hairpin structure. The two subunits are then connected by a disulfide bond. All of this combines to form a four alpha-helical bundle structure in aqueous solution. The toxin has a molecular weight of 7,928 Da. [2]

	== Subunits ==		== Subunits ==
Line 14:		Line 14:
	<b> Subunit A </b>		<b> Subunit A </b>
	<br>		<br>
-	1ECI.A has a 37 amino acid peptide sequence as followed: GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL [3]	+	1ECI.A has a 37 amino acid peptide sequence as followed: GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL [4]

	<b> Subunit B </b>		<b> Subunit B </b>
-	<br> 1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK [3]	+	<br> 1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK [4]


	== Function ==		== Function ==
-	<span> A toxin that blocks sodium or calcium channels are considered to be neurotoxins. [4] A study done on rat cardiac ventricular myocytes showed that the smallest presence of ectatomin decreases calcium currents in the body within seconds. After a few seconds the amount of calcium currents were reduced by half.	+	<span> A toxin that blocks sodium or calcium channels are considered to be neurotoxins. [5] A study done on rat cardiac ventricular myocytes showed that the smallest presence of ectatomin decreases calcium currents in the body within seconds. After a few seconds the amount of calcium currents were reduced by half.
-	When inserted into an artificial membrane, Ea forms an iron pore. Although it only requires 2 Ea molecules to form the pore, the formation of the pore requires reorganization of its helices. [3] [5]	+	When inserted into an artificial membrane, Ea forms an iron pore. Although it only requires 2 Ea molecules to form the pore, the formation of the pore requires reorganization of its helices. [4] [2]
-	There are two proposals as to how Ea forms pores. The first one, which is the most studied so far, is that a positively charged Ea molecule is concentrated close to a membrane, which then lowers the membrane's affinity. The membrane then breaks apart the two subunits and the hairpin sticks into the membrane, forming a pore. The second proposal is that the pore is formed by arranged Ea molecules in the membrane itself. [5]	+	There are two proposals as to how Ea forms pores. The first one, which is the most studied so far, is that a positively charged Ea molecule is concentrated close to a membrane, which then lowers the membrane's affinity. The membrane then breaks apart the two subunits and the hairpin sticks into the membrane, forming a pore. The second proposal is that the pore is formed by arranged whole Ea molecules in the membrane itself. [2]

	== Spectroscopy ==		== Spectroscopy ==
-	<span> 1ECI produces 20 H1 NMR structures. The 20 structures include the N- and c-termini. The rms deviations are 0.75 A for the heavy backbone atoms, and 1.25 A for all of the heavy atoms. [2]	+	<span> 1ECI produces 20 H1 NMR structures. The 20 structures include the N- and c-termini. The rms deviations are 0.75 A for the heavy backbone atoms, and 1.25 A for all of the heavy atoms. [3]


Line 37:		Line 37:
	1. Arseniev, A S, et al. "Toxic Principle of Selva Ant Venom Is a Pore-Forming Protein Transformer." FEBS Letters, vol. 347, no. 2-3, 27 June 1994, pp. 112-116. EBSCOhost, proxy.library.maryville.edu/login?url=https://search.ebscohost.com/login.aspx?direct=true&db=mdc&AN=8033986&site=eds-live&scope=site.		1. Arseniev, A S, et al. "Toxic Principle of Selva Ant Venom Is a Pore-Forming Protein Transformer." FEBS Letters, vol. 347, no. 2-3, 27 June 1994, pp. 112-116. EBSCOhost, proxy.library.maryville.edu/login?url=https://search.ebscohost.com/login.aspx?direct=true&db=mdc&AN=8033986&site=eds-live&scope=site.

-	2. ~~Nolde DE~~, ~~Sobol AG, Pluzhnikov KA, Grishin EV, Arseniev AS~~ (~~January 1995~~)~~. "Three-dimensional structure~~ of ~~ectatomin from Ectatomma tuberculatum~~ ant venom~~". J. Biomol. NMR. 5 (1): 1–13.~~ doi:10.~~1007~~/~~BF00227465. PMID 7881269.~~	+	2. Arseniev A.S, et al.(1994), Toxic principle of selva ant venom is a pore-forming protein transformer, FEBS Letters, 347, doi: 10.1016/0014-5793(94)00518-4

-	3. Pluzhnikov, ~~Kirill~~, ~~et al~~. ~~“Analysis~~ of ~~Ectatomin Action on Cell Membranes~~.~~” European Journal of Biochemistry 262~~.2 (~~1999~~):~~501~~. ~~Academic Search Complete~~. ~~Web~~. ~~13 Feb~~. ~~2017~~	+	3. Nolde DE, Sobol AG, Pluzhnikov KA, Grishin EV, Arseniev AS (January 1995). "Three-dimensional structure of ectatomin from Ectatomma tuberculatum ant venom". J. Biomol. NMR. 5 (1): 1–13. doi:10.1007/BF00227465. PMID 7881269.

-	4. Touchard, Axel, Samira R. Aili, Eduardo G. Fox, Pierre Escoubas, Jerome Orivel, Graham M. Nicholson, and Alain Dejuan. “The Biochemical Toxin Arsenal from Ant Venoms.” MDPI. N.p., 20 Jan. 2016. Web. 13 Feb. 2017.	+	4. Pluzhnikov, Kirill, et al. “Analysis of Ectatomin Action on Cell Membranes.” European Journal of Biochemistry 262.2 (1999):501. Academic Search Complete. Web. 13 Feb. 2017
		+
		+	5. Touchard, Axel, Samira R. Aili, Eduardo G. Fox, Pierre Escoubas, Jerome Orivel, Graham M. Nicholson, and Alain Dejuan. “The Biochemical Toxin Arsenal from Ant Venoms.” MDPI. N.p., 20 Jan. 2016. Web. 13 Feb. 2017.

Danelle Hale at 14:45, 2 May 2017

Danelle Hale — Tue, 02 May 2017 14:45:31 GMT

←Older revision		Revision as of 14:45, 2 May 2017
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	== ECTATOMIN 1ECI ==		== ECTATOMIN 1ECI ==
	<StructureSection load='1eci' size='340' side='right' caption='Ectatomin'</scene>		<StructureSection load='1eci' size='340' side='right' caption='Ectatomin'</scene>
-	Ectatomin is a water soluble toxic component from <i> Ectatomma tuberculatum </i> ant venom. It contains two homologous polypeptide chains with 37 and 34 residues, respectively. The chains are linked together by a disulfide bond. Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims.	+	Ectatomin (Ea) is a water soluble toxic component from <i> Ectatomma tuberculatum </i> ant venom. It contains two homologous polypeptide chains with 37 and 34 residues, respectively. The chains are linked together by a disulfide bond.[1] Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims. [4] Ectatomin is responsible for about 90% of the total toxicity of the venom produced by the ants. [5]
		+


	== Structure ==		== Structure ==
-	<span> Ectatomin is a dimeric peptide. Both subunits, A and B, are formed by two alpha-helixes and four residues forming a hinge region which all combine to form a hairpin structure. The two subunits are then connected by a disulfide bond. All of this combines to form a four alpha-helical bundle structure in aqueous solution.	+	<span> Ectatomin is a dimeric peptide. Both subunits, A and B, are formed by two alpha-helixes and four residues forming a hinge region which all combine to form a hairpin structure. The two subunits are then connected by a disulfide bond. All of this combines to form a four alpha-helical bundle structure in aqueous solution. The toxin has a molecular weight of 7,928 Da. [5]

	== Subunits ==		== Subunits ==
		+
		+	The peptide sequences are listed below. There are homologies between the two side chains, along with homologies to other proteins. [5]

	<b> Subunit A </b>		<b> Subunit A </b>
	<br>		<br>
-	1ECI.A has a 37 amino acid peptide sequence as followed: GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL	+	1ECI.A has a 37 amino acid peptide sequence as followed: GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL [3]

	<b> Subunit B </b>		<b> Subunit B </b>
-	<br> 1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK	+	<br> 1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK [3]


	== Function ==		== Function ==
-	<span> A study done on rat cardiac ventricular myocytes showed that the smallest presence of ectatomin decreases calcium currents in the body within seconds. After a few seconds the amount of calcium currents were reduced by half.	+	<span> A toxin that blocks sodium or calcium channels are considered to be neurotoxins. [4] A study done on rat cardiac ventricular myocytes showed that the smallest presence of ectatomin decreases calcium currents in the body within seconds. After a few seconds the amount of calcium currents were reduced by half.
-	When inserted into an artificial membrane, ~~ectatomin~~ forms an iron pore. ~~The~~ formation of the pore requires reorganization of its helices.	+	When inserted into an artificial membrane, Ea forms an iron pore. Although it only requires 2 Ea molecules to form the pore, the formation of the pore requires reorganization of its helices. [3] [5]
		+	There are two proposals as to how Ea forms pores. The first one, which is the most studied so far, is that a positively charged Ea molecule is concentrated close to a membrane, which then lowers the membrane's affinity. The membrane then breaks apart the two subunits and the hairpin sticks into the membrane, forming a pore. The second proposal is that the pore is formed by arranged Ea molecules in the membrane itself. [5]

	== Spectroscopy ==		== Spectroscopy ==
-	<span> 1ECI produces 20 H1 NMR structures. The 20 structures include the N- and c-termini. The rms deviations are 0.75 A for the heavy backbone atoms, and 1.25 A for all of the heavy atoms.	+	<span> 1ECI produces 20 H1 NMR structures. The 20 structures include the N- and c-termini. The rms deviations are 0.75 A for the heavy backbone atoms, and 1.25 A for all of the heavy atoms. [2]


Line 31:		Line 35:
	== References ==		== References ==
	<references/>		<references/>
-	Arseniev, A S, et al. "Toxic Principle of Selva Ant Venom Is a Pore-Forming Protein Transformer." FEBS Letters, vol. 347, no. 2-3, 27 June 1994, pp. 112-116. EBSCOhost, proxy.library.maryville.edu/login?url=https://search.ebscohost.com/login.aspx?direct=true&db=mdc&AN=8033986&site=eds-live&scope=site.	+	1. Arseniev, A S, et al. "Toxic Principle of Selva Ant Venom Is a Pore-Forming Protein Transformer." FEBS Letters, vol. 347, no. 2-3, 27 June 1994, pp. 112-116. EBSCOhost, proxy.library.maryville.edu/login?url=https://search.ebscohost.com/login.aspx?direct=true&db=mdc&AN=8033986&site=eds-live&scope=site.

-	Nolde DE, Sobol AG, Pluzhnikov KA, Grishin EV, Arseniev AS (January 1995). "Three-dimensional structure of ectatomin from Ectatomma tuberculatum ant venom". J. Biomol. NMR. 5 (1): 1–13. doi:10.1007/BF00227465. PMID 7881269.	+	2. Nolde DE, Sobol AG, Pluzhnikov KA, Grishin EV, Arseniev AS (January 1995). "Three-dimensional structure of ectatomin from Ectatomma tuberculatum ant venom". J. Biomol. NMR. 5 (1): 1–13. doi:10.1007/BF00227465. PMID 7881269.

-	Pluzhnikov, Kirill, et al. “Analysis of Ectatomin Action on Cell Membranes.” European Journal of Biochemistry 262.2 (1999):501. Academic Search Complete. Web. 13 Feb. 2017	+	3. Pluzhnikov, Kirill, et al. “Analysis of Ectatomin Action on Cell Membranes.” European Journal of Biochemistry 262.2 (1999):501. Academic Search Complete. Web. 13 Feb. 2017

-	Touchard, Axel, Samira R. Aili, Eduardo G. Fox, Pierre Escoubas, Jerome Orivel, Graham M. Nicholson, and Alain Dejuan. “The Biochemical Toxin Arsenal from Ant Venoms.” MDPI. N.p., 20 Jan. 2016. Web. 13 Feb. 2017.	+	4. Touchard, Axel, Samira R. Aili, Eduardo G. Fox, Pierre Escoubas, Jerome Orivel, Graham M. Nicholson, and Alain Dejuan. “The Biochemical Toxin Arsenal from Ant Venoms.” MDPI. N.p., 20 Jan. 2016. Web. 13 Feb. 2017.

Danelle Hale at 21:54, 26 April 2017

Danelle Hale — Wed, 26 Apr 2017 21:54:29 GMT

←Older revision		Revision as of 21:54, 26 April 2017
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	<b> Subunit B </b>		<b> Subunit B </b>
-	<br>	+	<br> 1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK
-	1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK	+

Danelle Hale at 19:39, 26 April 2017

Danelle Hale — Wed, 26 Apr 2017 19:39:58 GMT

←Older revision		Revision as of 19:39, 26 April 2017
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	== Subunits ==		== Subunits ==
		+
	<b> Subunit A </b>		<b> Subunit A </b>
	<br>		<br>

Danelle Hale at 19:26, 26 April 2017

Danelle Hale — Wed, 26 Apr 2017 19:26:06 GMT

←Older revision		Revision as of 19:26, 26 April 2017
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	== ECTATOMIN 1ECI ==		== ECTATOMIN 1ECI ==
-	<StructureSection load='1eci' size='340' side='right' caption='~~1ECI~~<~~Structure load='' size='350' frame='true' align='right' caption='Insert caption here'~~ scene~~='Insert optional scene name here' /~~>	+	<StructureSection load='1eci' size='340' side='right' caption='Ectatomin'</scene>
	Ectatomin is a water soluble toxic component from <i> Ectatomma tuberculatum </i> ant venom. It contains two homologous polypeptide chains with 37 and 34 residues, respectively. The chains are linked together by a disulfide bond. Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims.		Ectatomin is a water soluble toxic component from <i> Ectatomma tuberculatum </i> ant venom. It contains two homologous polypeptide chains with 37 and 34 residues, respectively. The chains are linked together by a disulfide bond. Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims.

Danelle Hale at 19:20, 26 April 2017

Danelle Hale — Wed, 26 Apr 2017 19:20:20 GMT

←Older revision		Revision as of 19:20, 26 April 2017
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	== Subunits ==		== Subunits ==
	<b> Subunit A </b>		<b> Subunit A </b>
		+	<br>
	1ECI.A has a 37 amino acid peptide sequence as followed: GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL		1ECI.A has a 37 amino acid peptide sequence as followed: GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL

	<b> Subunit B </b>		<b> Subunit B </b>
		+	<br>
	1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK		1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK

Danelle Hale at 18:42, 26 April 2017

Danelle Hale — Wed, 26 Apr 2017 18:42:17 GMT

←Older revision		Revision as of 18:42, 26 April 2017
Line 5:		Line 5:

	== Structure ==		== Structure ==
-	<span> Ectatomin is a dimeric peptide. Both subunits, A and B, are formed by two alpha-helixes and four residues forming a hinge region which all combine to form a hairpin structure. The two subunits are then connected by a disulfide bond. All of this combines to form a four alpha-helical bundle structure.	+	<span> Ectatomin is a dimeric peptide. Both subunits, A and B, are formed by two alpha-helixes and four residues forming a hinge region which all combine to form a hairpin structure. The two subunits are then connected by a disulfide bond. All of this combines to form a four alpha-helical bundle structure in aqueous solution.

	== Subunits ==		== Subunits ==

Danelle Hale at 18:40, 26 April 2017

Danelle Hale — Wed, 26 Apr 2017 18:40:19 GMT

←Older revision		Revision as of 18:40, 26 April 2017
Line 1:		Line 1:
	== ECTATOMIN 1ECI ==		== ECTATOMIN 1ECI ==
	<StructureSection load='1eci' size='340' side='right' caption='1ECI<Structure load='' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />		<StructureSection load='1eci' size='340' side='right' caption='1ECI<Structure load='' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
-	Ectatomin is a water soluble toxic component from <i> Ectatomma tuberculatum </b> ant venom. It contains two homologous polypeptide chains with 37 and 34 residues, respectively. The chains are linked together by a disulfide bond. Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims.	+	Ectatomin is a water soluble toxic component from <i> Ectatomma tuberculatum </i> ant venom. It contains two homologous polypeptide chains with 37 and 34 residues, respectively. The chains are linked together by a disulfide bond. Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims.

Danelle Hale at 18:40, 26 April 2017

Danelle Hale — Wed, 26 Apr 2017 18:40:00 GMT

←Older revision		Revision as of 18:40, 26 April 2017
Line 1:		Line 1:
	== ECTATOMIN 1ECI ==		== ECTATOMIN 1ECI ==
	<StructureSection load='1eci' size='340' side='right' caption='1ECI<Structure load='' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />		<StructureSection load='1eci' size='340' side='right' caption='1ECI<Structure load='' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
-	Ectatomin is a water soluble toxic component from Ectatomma tuberculatum ant venom. It contains two homologous polypeptide chains with 37 and 34 residues, respectively. The chains are linked together by a disulfide bond. Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims.	+	Ectatomin is a water soluble toxic component from <i> Ectatomma tuberculatum </b> ant venom. It contains two homologous polypeptide chains with 37 and 34 residues, respectively. The chains are linked together by a disulfide bond. Ectatomin in a cell leads to an irreversible increase in ion leakage, a decrease in membrane resistance, and eventually cell death. Ectatomin is found to be the most potent toxic peptide from ant venom because it blocks the calcium channel in the victims.


Line 9:		Line 9:
	== Subunits ==		== Subunits ==
	<b> Subunit A </b>		<b> Subunit A </b>
-	1ECI.A is has a 37 amino ~~aid~~ : GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL	+	1ECI.A has a 37 amino acid peptide sequence as followed: GVIPKKIWETVCPTVEPWAKKCSGDIATYIKRECGKL

	<b> Subunit B </b>		<b> Subunit B </b>
-	~~Has the protein~~ sequence: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK	+	1ECI.B has a 34 amino acid peptide sequence as followed: WSTIVKLTICPTLKSMAKKCEGSIATMIKKKCDK


	== Function ==		== Function ==
-	<span> ~~Ectatomin is~~ a calcium ~~channel blocker~~	+	<span> A study done on rat cardiac ventricular myocytes showed that the smallest presence of ectatomin decreases calcium currents in the body within seconds. After a few seconds the amount of calcium currents were reduced by half.
	When inserted into an artificial membrane, ectatomin forms an iron pore. The formation of the pore requires reorganization of its helices.		When inserted into an artificial membrane, ectatomin forms an iron pore. The formation of the pore requires reorganization of its helices.
		+
	== Spectroscopy ==		== Spectroscopy ==
	<span> 1ECI produces 20 H1 NMR structures. The 20 structures include the N- and c-termini. The rms deviations are 0.75 A for the heavy backbone atoms, and 1.25 A for all of the heavy atoms.		<span> 1ECI produces 20 H1 NMR structures. The 20 structures include the N- and c-termini. The rms deviations are 0.75 A for the heavy backbone atoms, and 1.25 A for all of the heavy atoms.