1yyj: Difference between revisions
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[[Image:1yyj.gif|left|200px]]<br /><applet load="1yyj" size=" | [[Image:1yyj.gif|left|200px]]<br /><applet load="1yyj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''The NMR solution structure of a redesigned apocytochrome b562:Rd-apocyt b562'''<br /> | '''The NMR solution structure of a redesigned apocytochrome b562:Rd-apocyt b562'''<br /> | ||
==Overview== | ==Overview== | ||
Structures of intermediates and transition states in protein folding are | 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== | ==About this Structure== | ||
1YYJ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | 1YYJ is a [http://en.wikipedia.org/wiki/Protein_complex 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14580191 14580191] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: BSGC, Berkeley | [[Category: BSGC, Berkeley Structural Genomics Center.]] | ||
[[Category: Bai, Y.]] | [[Category: Bai, Y.]] | ||
[[Category: Feng, H.]] | [[Category: Feng, H.]] | ||
| Line 25: | Line 25: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:24 2008'' | ||
Revision as of 17:10, 21 February 2008
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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
1YYJ is a Protein complex structure of sequences from [1]. 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
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