NMR Structure Determination Of Toxin b
碩士 === 國立清華大學 === 化學學系 === 84 === The solution structure of Toxin b, a long neurotoxin ( 73 no acids and five disulfides) , from the venom of Ophiophagus hannah( King Cobra) has been determined using 1H NMR and modeling. The structures wer...
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ndltd-TW-084NTHU00650682016-07-13T04:10:34Z http://ndltd.ncl.edu.tw/handle/92791648917678551684 NMR Structure Determination Of Toxin b 眼鏡蛇王神經毒蛋白之水溶液結構研究 Shi-Shung Peng 彭世熊 碩士 國立清華大學 化學學系 84 The solution structure of Toxin b, a long neurotoxin ( 73 no acids and five disulfides) , from the venom of Ophiophagus hannah( King Cobra) has been determined using 1H NMR and modeling. The structures were calculated using 415 distance constraints and 52 dihedral angle restraints. The average atoms RMSD between the twelve refined structures and the mean structure is 0.7 ?for the backbone heavy atoms, and 3.1for all the heavy atoms. The protein consists of a core region from which three finger like loops extend outwards. The secondary structure includes a short double and a triple antiparallel b sheets. Comparison with the solution structures of other long neurotoxins indicates that the structure of toxin b is quite similar to previously reported long neurotoxin structures but clear local structural differences are observed in regions thought to be for binding of neurotoxins to the acetylcholine receptor (AChR). Loop II, which is important for the binding of the toxin to the acetylcholine receptor is shorter in toxin b as compared to the other long neurotoxins and the tip of Loop II has a well defined local structure. Yu Chin 余靖 1996 學位論文 ; thesis 105 zh-TW |
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碩士 === 國立清華大學 === 化學學系 === 84 === The solution structure of Toxin b, a long neurotoxin ( 73 no
acids and five disulfides) , from the venom of Ophiophagus
hannah( King Cobra) has been determined using 1H NMR and
modeling. The structures were calculated using 415 distance
constraints and 52 dihedral angle restraints. The average atoms
RMSD between the twelve refined structures and the mean
structure is 0.7 ?for the backbone heavy atoms, and 3.1for
all the heavy atoms. The protein consists of a core region from
which three finger like loops extend outwards. The secondary
structure includes a short double and a triple antiparallel b
sheets. Comparison with the solution structures of other long
neurotoxins indicates that the structure of toxin b is quite
similar to previously reported long neurotoxin structures but
clear local structural differences are observed in regions
thought to be for binding of neurotoxins to the acetylcholine
receptor (AChR). Loop II, which is important for the binding of
the toxin to the acetylcholine receptor is shorter in toxin b
as compared to the other long neurotoxins and the tip of Loop
II has a well defined local structure.
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author2 |
Yu Chin |
author_facet |
Yu Chin Shi-Shung Peng 彭世熊 |
author |
Shi-Shung Peng 彭世熊 |
spellingShingle |
Shi-Shung Peng 彭世熊 NMR Structure Determination Of Toxin b |
author_sort |
Shi-Shung Peng |
title |
NMR Structure Determination Of Toxin b |
title_short |
NMR Structure Determination Of Toxin b |
title_full |
NMR Structure Determination Of Toxin b |
title_fullStr |
NMR Structure Determination Of Toxin b |
title_full_unstemmed |
NMR Structure Determination Of Toxin b |
title_sort |
nmr structure determination of toxin b |
publishDate |
1996 |
url |
http://ndltd.ncl.edu.tw/handle/92791648917678551684 |
work_keys_str_mv |
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