1yyj
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1yyj.gif|left|200px]] | + | [[Image:1yyj.gif|left|200px]] |
| - | + | ||
| - | '''The NMR solution structure of a redesigned apocytochrome b562:Rd-apocyt b562''' | + | {{Structure |
| + | |PDB= 1yyj |SIZE=350|CAPTION= <scene name='initialview01'>1yyj</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''The NMR solution structure of a redesigned apocytochrome b562:Rd-apocyt b562''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1YYJ is a [ | + | 1YYJ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYJ OCA]. |
==Reference== | ==Reference== | ||
| - | Specific non-native hydrophobic interactions in a hidden folding intermediate: implications for protein folding., Feng H, Takei J, Lipsitz R, Tjandra N, Bai Y, Biochemistry. 2003 Nov 4;42(43):12461-5. PMID:[http:// | + | Specific non-native hydrophobic interactions in a hidden folding intermediate: implications for protein folding., Feng H, Takei J, Lipsitz R, Tjandra N, Bai Y, Biochemistry. 2003 Nov 4;42(43):12461-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14580191 14580191] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: BSGC, Berkeley Structural Genomics Center.]] | [[Category: BSGC, Berkeley Structural Genomics Center.]] | ||
| Line 23: | Line 32: | ||
[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:29:04 2008'' |
Revision as of 13:29, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The NMR solution structure of a redesigned apocytochrome b562:Rd-apocyt b562
Overview
Structures of intermediates and transition states in protein folding are usually characterized by amide hydrogen exchange and protein engineering methods and interpreted on the basis of the assumption that they have native-like conformations. We were able to stabilize and determine the high-resolution structure of a partially unfolded intermediate that exists after the rate-limiting step of a four-helix bundle protein, Rd-apocyt b(562), by multidimensional NMR methods. The intermediate has partial native-like secondary structure and backbone topology, consistent with our earlier native state hydrogen exchange results. However, non-native hydrophobic interactions exist throughout the structure. These and other results in the literature suggest that non-native hydrophobic interactions may occur generally in partially folded states. This can alter the interpretation of mutational protein engineering results in terms of native-like side chain interactions. In addition, since the intermediate exists after the rate-limiting step and Rd-apocyt b(562) folds very rapidly (k(f) approximately 10(4) s(-1)), these results suggest that non-native hydrophobic interactions, in the absence of topological misfolding, are repaired too rapidly to slow folding and cause the accumulation of folding intermediates. More generally, these results illustrate an approach for determining the high-resolution structure of folding intermediates.
About this Structure
1YYJ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Specific non-native hydrophobic interactions in a hidden folding intermediate: implications for protein folding., Feng H, Takei J, Lipsitz R, Tjandra N, Bai Y, Biochemistry. 2003 Nov 4;42(43):12461-5. PMID:14580191
Page seeded by OCA on Thu Mar 20 15:29:04 2008
