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[[Image:1yza.gif|left|200px]]
{{Seed}}
[[Image:1yza.png|left|200px]]


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{{STRUCTURE_1yza|  PDB=1yza  |  SCENE=  }}  
{{STRUCTURE_1yza|  PDB=1yza  |  SCENE=  }}  


'''The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N-terminal helix unfolded'''
===The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N-terminal helix unfolded===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_14580191}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 14580191 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14580191}}


==About this Structure==
==About this Structure==
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZA OCA].  
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZA OCA].  


==Reference==
==Reference==
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[[Category: Rd-apocyt b562]]
[[Category: Rd-apocyt b562]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:59:41 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:28:34 2008''

Revision as of 16:28, 28 July 2008

File:1yza.png

Template:STRUCTURE 1yza

The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N-terminal helix unfolded

Template:ABSTRACT PUBMED 14580191

About this Structure

Full experimental 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

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