Three-dimensional structure of phoratoxin in solution: combined use of nuclear magnetic resonance, distance geometry, and restrained molecular dynamics

Biochemistry ◽  
1987 ◽  
Vol 26 (6) ◽  
pp. 1732-1745 ◽  
Author(s):  
G. Marius Clore ◽  
Dinesh K. Sukumaran ◽  
Michael Nilges ◽  
Angela M. Gronenborn
Keyword(s):  
Molecular Dynamics ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Distance Geometry ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Combined Use ◽  
Restrained Molecular Dynamics ◽  
Nuclear Magnetic

scholarly journals The three-dimensional structure of α1-purothionin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics

1986 ◽  
Vol 5 (10) ◽  
pp. 2729-2735 ◽  
Author(s):  
G. Marius Clore ◽  
Michael Nilges ◽  
Dinesh K. Sukumaran ◽  
Axel T. Brünger ◽  
Martin Karplus ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Distance Geometry ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Combined Use ◽  
Restrained Molecular Dynamics ◽  
Nuclear Magnetic

Refinement of the solution structure of the DNA dodecamer 5'd(CGCGPATTCGCG)2 containing a stable purine-thymine base pair: combined use of nuclear magnetic resonance and restrained molecular dynamics

Biochemistry ◽  
1988 ◽  
Vol 27 (11) ◽  
pp. 4185-4197 ◽  
Author(s):  
G. Marius Clore ◽  
Hartmut Oschkinat ◽  
Larry W. McLaughlin ◽  
Fritz Benseler ◽  
Claudia Scalfi Happ ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Base Pair ◽  
Solution Structure ◽  
Combined Use ◽  
Dna Dodecamer ◽  
Restrained Molecular Dynamics ◽  
Nuclear Magnetic

scholarly journals Nuclear Magnetic Resonance seq (NMRseq): A New Approach to Peptide Sequence Tags

Toxins ◽  
2018 ◽  
Vol 10 (11) ◽  
pp. 437 ◽  
Author(s):  
David Wilson ◽  
Norelle L. Daly
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Nmr Spectroscopy ◽  
Magnetic Resonance ◽  
De Novo ◽  
Three Dimensional ◽  
Peptide Sequence ◽  
Dimensional Structure ◽  
Amino Acid Type ◽  
Three Dimensional Structure ◽  
Nuclear Magnetic

Structural analysis of peptides with nuclear magnetic resonance (NMR) spectroscopy generally relies on knowledge of the primary sequence to enable assignment of the resonances prior to determination of the three-dimensional structure. Resonance assignment without knowledge of the sequence is complicated by redundancy in amino acid type, making complete de novo sequencing using NMR spectroscopy unlikely to be feasible. Despite this redundancy, we show here that NMR spectroscopy can be used to identify short sequence tags that can be used to elucidate full-length peptide sequences via database searching. In the current study, we have used this approach to identify conotoxins from the venom of the cone snail Conus geographus and determined the three-dimensional structure of a member of the I3 superfamily. This approach is most likely to be useful for the characterization of disulfide-rich peptides, such as those that were chosen for this study, as they generally have well-defined structures, which enhances the quality of the NMR spectra. In contrast to other sequencing methods, the lack of sample manipulation, such as protease digestion, allows for subsequent bioassays to be carried out using the native sample used for sequence identification.

scholarly journals The conformations of hirudin in solution: a study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics

1987 ◽  
Vol 6 (2) ◽  
pp. 529-537 ◽  
Author(s):  
G. Marius Clore ◽  
Dinesh K. Sukumaran ◽  
Michael Nilges ◽  
Jutta Zarbock ◽  
Angela M. Gronenborn
Keyword(s):  
Molecular Dynamics ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Distance Geometry ◽  
Restrained Molecular Dynamics ◽  
Nuclear Magnetic
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