1yyj: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1yyj.gif|left|200px]] | [[Image:1yyj.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1yyj", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1yyj| PDB=1yyj | SCENE= }} | |||
}} | |||
'''The NMR solution structure of a redesigned apocytochrome b562:Rd-apocyt b562''' | '''The NMR solution structure of a redesigned apocytochrome b562:Rd-apocyt b562''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
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://www.ncbi.nlm.nih.gov/pubmed/14580191 14580191] | 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: BSGC, Berkeley Structural Genomics Center.]] | [[Category: BSGC, Berkeley Structural Genomics Center.]] | ||
[[Category: Bai, Y.]] | [[Category: Bai, Y.]] | ||
| Line 30: | Line 26: | ||
[[Category: Takei, J.]] | [[Category: Takei, J.]] | ||
[[Category: Tjandra, N.]] | [[Category: Tjandra, N.]] | ||
[[Category: | [[Category: Berkeley structural genomics center]] | ||
[[Category: | [[Category: Bsgc]] | ||
[[Category: | [[Category: Four helix protein]] | ||
[[Category: | [[Category: Protein structure initiative]] | ||
[[Category: | [[Category: Psi]] | ||
[[Category: | [[Category: Structural genomic]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:57:51 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 16:57, 3 May 2008
The NMR solution structure of a redesigned apocytochrome b562:Rd-apocyt b562
OverviewOverview
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 StructureAbout this Structure
Full crystallographic information is available from OCA.
ReferenceReference
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 Sat May 3 16:57:51 2008