Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding

Biochemistry ◽  
1992 ◽  
Vol 31 (26) ◽  
pp. 5974-5983 ◽  
Author(s):  
Magnus Ullner ◽  
Maria Selander ◽  
Egon Persson ◽  
Johan Stenflo ◽  
Torbjoern Drakenberg ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Blood Coagulation ◽  
Three Dimensional ◽  
Coagulation Factor ◽  
Dimensional Structure ◽  
Factor X ◽  
Three Dimensional Structure

The three-dimensional structure of the vnd/NK-2 homeodomain-DNA complex by NMR spectroscopy

1999 ◽  
Vol 289 (3) ◽  
pp. 529-545 ◽  
Author(s):  
James M. Gruschus ◽  
Désirée H.H. Tsao ◽  
Lan-Hsiang Wang ◽  
Marshall Nirenberg ◽  
James A. Ferretti
Keyword(s):  
Nmr Spectroscopy ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Dna Complex

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.

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