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Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations.
Single-chain monellin (SCM), which is an engineered 94-residue polypeptide, has proven to be as sweet as native two-chain monellin. SCM is more stable than the native monellin for both heat and acidic environments. Data from gel filtration HPLC and NMR indicate that the SCM exists as a monomer in aqueous solution. The solution structure of SCM has been determined by nuclear magnetic resonance (NMR) spectroscopy and dynamical simulated annealing calculations. A stable alpha-helix spanning residues Phe11-Ile26 and an antiparallel beta-sheet formed by residues 2-5, 36-38, 41-47, 54-64, 69-75, and 83-88 have been identified. The sheet was well defined by backbone-backbone NOEs, and the corresponding beta-strands were further confirmed by hydrogen bond networks based on amide hydrogen exchange data. Strands beta2 and beta3 are connected by a small bulge comprising residues Ile38-Cys41. A total of 993 distance and 56 dihedral angle restraints were used for simulated annealing calculations. The final simulated annealing structures (
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Related Subject Headings
- Thermodynamics
- Sweetening Agents
- Solutions
- Protein Structure, Secondary
- Plant Proteins
- Nuclear Magnetic Resonance, Biomolecular
- Molecular Sequence Data
- Models, Molecular
- Mathematical Computing
- Crystallography, X-Ray
Citation
![Journal cover image](https://secure.syndetics.com/index.aspx?isbn=/lc.gif&issn=0006-2960&client=dukeuniv)
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Thermodynamics
- Sweetening Agents
- Solutions
- Protein Structure, Secondary
- Plant Proteins
- Nuclear Magnetic Resonance, Biomolecular
- Molecular Sequence Data
- Models, Molecular
- Mathematical Computing
- Crystallography, X-Ray