Abstract
The solution conformation of a synthetic snake venom toxin waglerin I, has been determined by using proton nuclear magnetic resonance spectroscopy. By a combination of various two-dimensional NMR techniques, the 1H-NMR spectrum of waglerin I was completely assigned. A set of 247 interproton distance restraints was derived from nuclear Overhauser enhancement (NOE) measurements. These NOE constraints, in addition to the 2 dihedral angle restraints (from coupling constant measurements) and 7 ω torsion angle restraints for prolines, formed the basis of three-dimensional structure determined by molecular dynamics techniques. The 19 structures that were obtained satisfy the experimental restraints, and display small deviation from idealized covalent geometry. Analysis of converged structures indicates that the toxin has no special secondary structure. In the solution structure of waglerin I, the central ring region is well defined but the N- and C-termini possesses more disorder.
| Original language | English |
|---|---|
| Pages (from-to) | 145-155 |
| Number of pages | 11 |
| Journal | Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology |
| Volume | 1292 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 1996 Jan 4 |
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Keywords
- Molecular dynamics simulation
- Nuclear magnetic resonance
- Protein solution structure
- Snake venom
- T. wagleri
- Waglerin
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
Cite this
Determination of three-dimensional solution structure of waglerin I, a toxin from Trimeresurus wagleri, using 2D-NMR and molecular dynamics simulation. / Chuang, Li Chin; Yu, Hui Ming; Chen, Chinpan; Huang, Tai Huang; Wu, Shih Hsiung; Wang, Kung Tsung.
In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, Vol. 1292, No. 1, 04.01.1996, p. 145-155.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Determination of three-dimensional solution structure of waglerin I, a toxin from Trimeresurus wagleri, using 2D-NMR and molecular dynamics simulation
AU - Chuang, Li Chin
AU - Yu, Hui Ming
AU - Chen, Chinpan
AU - Huang, Tai Huang
AU - Wu, Shih Hsiung
AU - Wang, Kung Tsung
PY - 1996/1/4
Y1 - 1996/1/4
N2 - The solution conformation of a synthetic snake venom toxin waglerin I, has been determined by using proton nuclear magnetic resonance spectroscopy. By a combination of various two-dimensional NMR techniques, the 1H-NMR spectrum of waglerin I was completely assigned. A set of 247 interproton distance restraints was derived from nuclear Overhauser enhancement (NOE) measurements. These NOE constraints, in addition to the 2 dihedral angle restraints (from coupling constant measurements) and 7 ω torsion angle restraints for prolines, formed the basis of three-dimensional structure determined by molecular dynamics techniques. The 19 structures that were obtained satisfy the experimental restraints, and display small deviation from idealized covalent geometry. Analysis of converged structures indicates that the toxin has no special secondary structure. In the solution structure of waglerin I, the central ring region is well defined but the N- and C-termini possesses more disorder.
AB - The solution conformation of a synthetic snake venom toxin waglerin I, has been determined by using proton nuclear magnetic resonance spectroscopy. By a combination of various two-dimensional NMR techniques, the 1H-NMR spectrum of waglerin I was completely assigned. A set of 247 interproton distance restraints was derived from nuclear Overhauser enhancement (NOE) measurements. These NOE constraints, in addition to the 2 dihedral angle restraints (from coupling constant measurements) and 7 ω torsion angle restraints for prolines, formed the basis of three-dimensional structure determined by molecular dynamics techniques. The 19 structures that were obtained satisfy the experimental restraints, and display small deviation from idealized covalent geometry. Analysis of converged structures indicates that the toxin has no special secondary structure. In the solution structure of waglerin I, the central ring region is well defined but the N- and C-termini possesses more disorder.
KW - Molecular dynamics simulation
KW - Nuclear magnetic resonance
KW - Protein solution structure
KW - Snake venom
KW - T. wagleri
KW - Waglerin
UR - http://www.scopus.com/inward/record.url?scp=0030029475&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030029475&partnerID=8YFLogxK
U2 - 10.1016/0167-4838(95)00181-6
DO - 10.1016/0167-4838(95)00181-6
M3 - Article
C2 - 8547337
AN - SCOPUS:0030029475
VL - 1292
SP - 145
EP - 155
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
SN - 1570-9639
IS - 1
ER -