1ter
From Proteopedia
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'''SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY''' | '''SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY''' | ||
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[[Category: Nelson, J W.]] | [[Category: Nelson, J W.]] | ||
[[Category: Xu, X.]] | [[Category: Xu, X.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:51:44 2008'' | |
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Revision as of 06:51, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 09:51:44 2008
