1mol
From Proteopedia
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===TWO CRYSTAL STRUCTURES OF A POTENTLY SWEET PROTEIN: NATURAL MONELLIN AT 2.75 ANGSTROMS RESOLUTION AND SINGLE-CHAIN MONELLIN AT 1.7 ANGSTROMS RESOLUTION=== | ===TWO CRYSTAL STRUCTURES OF A POTENTLY SWEET PROTEIN: NATURAL MONELLIN AT 2.75 ANGSTROMS RESOLUTION AND SINGLE-CHAIN MONELLIN AT 1.7 ANGSTROMS RESOLUTION=== | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | [[1mol]] is a 2 chain structure with 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=1MOL OCA]. | |
==Reference== | ==Reference== | ||
| - | + | <ref group="xtra">PMID:008230222</ref><ref group="xtra">PMID:011742118</ref><ref group="xtra">PMID:011880627</ref><ref group="xtra">PMID:014695246</ref><references group="xtra"/> | |
[[Category: Dioscoreophyllum cumminsii]] | [[Category: Dioscoreophyllum cumminsii]] | ||
| - | [[Category: Single protein]] | ||
[[Category: Kim, S H.]] | [[Category: Kim, S H.]] | ||
[[Category: Somoza, J R.]] | [[Category: Somoza, J R.]] | ||
[[Category: Sweet-tasting protein]] | [[Category: Sweet-tasting protein]] | ||
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Revision as of 15:12, 14 August 2012
TWO CRYSTAL STRUCTURES OF A POTENTLY SWEET PROTEIN: NATURAL MONELLIN AT 2.75 ANGSTROMS RESOLUTION AND SINGLE-CHAIN MONELLIN AT 1.7 ANGSTROMS RESOLUTION
Template:ABSTRACT PUBMED 8230222
About this Structure
1mol is a 2 chain structure with sequence from Dioscoreophyllum cumminsii. Full crystallographic information is available from OCA.
Reference
- Somoza JR, Jiang F, Tong L, Kang CH, Cho JM, Kim SH. Two crystal structures of a potently sweet protein. Natural monellin at 2.75 A resolution and single-chain monellin at 1.7 A resolution. J Mol Biol. 1993 Nov 20;234(2):390-404. PMID:8230222 doi:http://dx.doi.org/S0022-2836(83)71594-9
- Shortle D. Composites of local structure propensities: evidence for local encoding of long-range structure. Protein Sci. 2002 Jan;11(1):18-26. PMID:11742118
- Richardson JS, Richardson DC. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2754-9. PMID:11880627 doi:10.1073/pnas.052706099
- Sandelin E. On hydrophobicity and conformational specificity in proteins. Biophys J. 2004 Jan;86(1 Pt 1):23-30. PMID:14695246 doi:10.1016/S0006-3495(04)74080-1
