1ter

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(New page: 200px<br /><applet load="1ter" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ter" /> '''SOLUTION STRUCTURE OF TERTIAPIN DETERMINED U...)
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[[Image:1ter.gif|left|200px]]<br /><applet load="1ter" size="350" color="white" frame="true" align="right" spinBox="true"
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'''SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY'''<br />
'''SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY'''<br />
==Overview==
==Overview==
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The solution structure of tertiapin, a 21-residue bee venom peptide, has, been characterized by circular dichroism (CD), two-dimensional nuclear, magnetic resonance (NMR) spectroscopy, and distance geometry. A total of, 21 lowest error structures were obtained from distance geometry, calculations. Superimposition of these structures shows that the backbone, of tertiapin is very well defined. One type-I reverse turn from residue 4, to 7 and an alpha-helix from residue 12 to 19 exist in the structure of, tertiapin. The alpha-helical region is best defined from both, conformational analysis and structural superimposition. The overall, three-dimensional structure of tertiapin is highly compact resulting from, side chain interactions. The structural information obtained from CD and, NMR are compared for both tertiapin and apamin (ref. 3), another bee venom, peptide. Tertiapin and apamin have some similar secondary structure, but, display different tertiary structures.
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The solution structure of tertiapin, a 21-residue bee venom peptide, has been characterized by circular dichroism (CD), two-dimensional nuclear magnetic resonance (NMR) spectroscopy, and distance geometry. A total of 21 lowest error structures were obtained from distance geometry calculations. Superimposition of these structures shows that the backbone of tertiapin is very well defined. One type-I reverse turn from residue 4 to 7 and an alpha-helix from residue 12 to 19 exist in the structure of tertiapin. The alpha-helical region is best defined from both conformational analysis and structural superimposition. The overall three-dimensional structure of tertiapin is highly compact resulting from side chain interactions. The structural information obtained from CD and NMR are compared for both tertiapin and apamin (ref. 3), another bee venom peptide. Tertiapin and apamin have some similar secondary structure, but display different tertiary structures.
==About this Structure==
==About this Structure==
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1TER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TER OCA].
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1TER is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TER OCA].
==Reference==
==Reference==
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[[Category: Apis mellifera]]
[[Category: Apis mellifera]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Nelson, J.W.]]
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[[Category: Nelson, J W.]]
[[Category: Xu, X.]]
[[Category: Xu, X.]]
[[Category: NH2]]
[[Category: NH2]]
[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:12:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:45 2008''

Revision as of 13:12, 21 February 2008

Image:1ter.gif

1ter

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SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY

Overview

The solution structure of tertiapin, a 21-residue bee venom peptide, has been characterized by circular dichroism (CD), two-dimensional nuclear magnetic resonance (NMR) spectroscopy, and distance geometry. A total of 21 lowest error structures were obtained from distance geometry calculations. Superimposition of these structures shows that the backbone of tertiapin is very well defined. One type-I reverse turn from residue 4 to 7 and an alpha-helix from residue 12 to 19 exist in the structure of tertiapin. The alpha-helical region is best defined from both conformational analysis and structural superimposition. The overall three-dimensional structure of tertiapin is highly compact resulting from side chain interactions. The structural information obtained from CD and NMR are compared for both tertiapin and apamin (ref. 3), another bee venom peptide. Tertiapin and apamin have some similar secondary structure, but display different tertiary structures.

About this Structure

1TER is a Single protein structure of sequence from Apis mellifera with as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of tertiapin determined using nuclear magnetic resonance and distance geometry., Xu X, Nelson JW, Proteins. 1993 Oct;17(2):124-37. PMID:8265561

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