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1mnl

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{{STRUCTURE_1mnl| PDB=1mnl | SCENE= }}
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'''HIGH-RESOLUTION SOLUTION STRUCTURE OF A SWEET PROTEIN SINGLE-CHAIN MONELLIN (SCM) DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY AND DYNAMICAL SIMULATED ANNEALING CALCULATIONS, 21 STRUCTURES'''
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===HIGH-RESOLUTION SOLUTION STRUCTURE OF A SWEET PROTEIN SINGLE-CHAIN MONELLIN (SCM) DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY AND DYNAMICAL SIMULATED ANNEALING CALCULATIONS, 21 STRUCTURES===
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==Overview==
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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 (&lt;SA&gt;k) converged well with a root-mean-square deviation (rmsd) between backbone atoms of 0.49 A for secondary structural regions and 0.70 A for backbone atoms excluding two loop regions. The average restraint energy-minimized (REM) structure exhibited root-mean-square deviations of 1.19 A for backbone atoms and 0.85 A for backbone atoms excluding two loop regions with respect to 20 &lt;SA&gt;k structures. The solution structure of SCM revealed that the long alpha-helix was folded into the concave side of a six-stranded antiparallel beta-sheet. The side chains of Tyr63 and Asp66 which are common to all sweet peptides showed an opposite orientation relative to H1 helix, and they were all solvent-exposed. Residues at the proposed dimeric interface in the X-ray structure were observed to be mostly solvent-exposed and demonstrated high degrees of flexibility.
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{{ABSTRACT_PUBMED_10029527}}
==About this Structure==
==About this Structure==
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1MNL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dioscoreophyllum_cumminsii Dioscoreophyllum cumminsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNL OCA].
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1MNL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dioscoreophyllum_cumminsii Dioscoreophyllum cumminsii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNL OCA].
==Reference==
==Reference==
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[[Category: Sweet protein]]
[[Category: Sweet protein]]
[[Category: Sweet receptor binding]]
[[Category: Sweet receptor binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:27:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:28:55 2008''

Revision as of 21:28, 2 July 2008

Image:1mnl.png

Template:STRUCTURE 1mnl

HIGH-RESOLUTION SOLUTION STRUCTURE OF A SWEET PROTEIN SINGLE-CHAIN MONELLIN (SCM) DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY AND DYNAMICAL SIMULATED ANNEALING CALCULATIONS, 21 STRUCTURES

Template:ABSTRACT PUBMED 10029527

About this Structure

1MNL is a Single protein structure of sequence from Dioscoreophyllum cumminsii. Full experimental information is available from OCA.

Reference

Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations., Lee SY, Lee JH, Chang HJ, Cho JM, Jung JW, Lee W, Biochemistry. 1999 Feb 23;38(8):2340-6. PMID:10029527

Page seeded by OCA on Thu Jul 3 00:28:55 2008

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