1wit: Difference between revisions

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[[Image:1wit.jpg|left|200px]]<br /><applet load="1wit" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1wit.jpg|left|200px]]<br /><applet load="1wit" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1wit" />

'''TWITCHIN IMMUNOGLOBULIN SUPERFAMILY DOMAIN (IGSF MODULE) (IG 18'), NMR, MINIMIZED AVERAGE STRUCTURE'''<br />

==Overview==

The NMR solution structure of an immunoglobulin superfamily module of, twitchin (Ig 18') has been determined and the kinetic and equilibrium, folding behaviour characterised. Thirty molecular coordinates were, calculated using a hybrid distance geometry-simulated annealing protocol, based on 1207 distance and 48 dihedral restraints. The atomic rms, distributions about the mean coordinate for the ensemble of structures is, 0.55( +/- 0.09) A for backbone atoms and 1.10( +/- 0.08) A for all heavy, atoms. The protein has a topology very similar to that of telokin and the, titin Ig domains and thus it falls into the I set of the immunoglobulin, superfamily. The close agreement between the predicted and observed, structures of Ig 18' demonstrates clearly that the I set profile can be, applied in the structure prediction of immunoglobulin-like domains of, diverse modular proteins. Folding studies reveal that the protein has, relatively low thermodynamic stability, deltaG(H2O)U-F = 4.0 kcal mol(-1), at physiological pH. Unfolding studies suggest that the protein has, considerable kinetic stability, the half life of the unfolding is greater, than 40 minutes in the absence of denaturant.

The NMR solution structure of an immunoglobulin superfamily module of twitchin (Ig 18') has been determined and the kinetic and equilibrium folding behaviour characterised. Thirty molecular coordinates were calculated using a hybrid distance geometry-simulated annealing protocol based on 1207 distance and 48 dihedral restraints. The atomic rms distributions about the mean coordinate for the ensemble of structures is 0.55( +/- 0.09) A for backbone atoms and 1.10( +/- 0.08) A for all heavy atoms. The protein has a topology very similar to that of telokin and the titin Ig domains and thus it falls into the I set of the immunoglobulin superfamily. The close agreement between the predicted and observed structures of Ig 18' demonstrates clearly that the I set profile can be applied in the structure prediction of immunoglobulin-like domains of diverse modular proteins. Folding studies reveal that the protein has relatively low thermodynamic stability, deltaG(H2O)U-F = 4.0 kcal mol(-1) at physiological pH. Unfolding studies suggest that the protein has considerable kinetic stability, the half life of the unfolding is greater than 40 minutes in the absence of denaturant.

==About this Structure==

1WIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1WIT OCA].

1WIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WIT OCA].

==Reference==

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[[Category: muscle protein]]

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@@ Line 1: / Line 1: @@
-[[Image:1wit.jpg|left|200px]]<br /><applet load="1wit" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1wit.jpg|left|200px]]<br /><applet load="1wit" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1wit" />
 '''TWITCHIN IMMUNOGLOBULIN SUPERFAMILY DOMAIN (IGSF MODULE) (IG 18'), NMR, MINIMIZED AVERAGE STRUCTURE'''<br />
 ==Overview==
-The NMR solution structure of an immunoglobulin superfamily module of, twitchin (Ig 18') has been determined and the kinetic and equilibrium, folding behaviour characterised. Thirty molecular coordinates were, calculated using a hybrid distance geometry-simulated annealing protocol, based on 1207 distance and 48 dihedral restraints. The atomic rms, distributions about the mean coordinate for the ensemble of structures is, 0.55( +/- 0.09) A for backbone atoms and 1.10( +/- 0.08) A for all heavy, atoms. The protein has a topology very similar to that of telokin and the, titin Ig domains and thus it falls into the I set of the immunoglobulin, superfamily. The close agreement between the predicted and observed, structures of Ig 18' demonstrates clearly that the I set profile can be, applied in the structure prediction of immunoglobulin-like domains of, diverse modular proteins. Folding studies reveal that the protein has, relatively low thermodynamic stability, deltaG(H2O)U-F = 4.0 kcal mol(-1), at physiological pH. Unfolding studies suggest that the protein has, considerable kinetic stability, the half life of the unfolding is greater, than 40 minutes in the absence of denaturant.
+The NMR solution structure of an immunoglobulin superfamily module of twitchin (Ig 18') has been determined and the kinetic and equilibrium folding behaviour characterised. Thirty molecular coordinates were calculated using a hybrid distance geometry-simulated annealing protocol based on 1207 distance and 48 dihedral restraints. The atomic rms distributions about the mean coordinate for the ensemble of structures is 0.55( +/- 0.09) A for backbone atoms and 1.10( +/- 0.08) A for all heavy atoms. The protein has a topology very similar to that of telokin and the titin Ig domains and thus it falls into the I set of the immunoglobulin superfamily. The close agreement between the predicted and observed structures of Ig 18' demonstrates clearly that the I set profile can be applied in the structure prediction of immunoglobulin-like domains of diverse modular proteins. Folding studies reveal that the protein has relatively low thermodynamic stability, deltaG(H2O)U-F = 4.0 kcal mol(-1) at physiological pH. Unfolding studies suggest that the protein has considerable kinetic stability, the half life of the unfolding is greater than 40 minutes in the absence of denaturant.
 ==About this Structure==
-WIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WIT OCA].
+WIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WIT OCA].
 ==Reference==
@@ Line 19: / Line 19: @@
 [[Category: muscle protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:00:59 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:44:49 2008''