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[[Image:1yyx.gif|left|200px]]
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[[Image:1yyx.png|left|200px]]


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{{STRUCTURE_1yyx|  PDB=1yyx  |  SCENE=  }}  
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'''The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) at 2.8M urea'''
===The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) at 2.8M urea===




==Overview==
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The absence of detectable kinetic and equilibrium folding intermediates by optical probes is commonly taken to indicate that protein folding is a two-state process. However, for some small proteins with apparent two-state behavior, unfolding intermediates have been identified in native-state hydrogen exchange or kinetic unfolding experiments monitored by nuclear magnetic resonance. Rd-apocytochrome b(562), a four-helix bundle, is one such protein. Here, we found another unfolding intermediate for Rd-apocytochrome b(562). It is based on a cooperative transition of (15)N chemical shifts of amide protons as a function of urea concentrations before the global unfolding. We have solved the high-resolution structure of the protein at 2.8 M urea, which is after this cooperative transition but before the global unfolding. All four helices remained intact, but a number of hydrophobic core residues repacked. This intermediate provides a possible structural interpretation for the kinetic unfolding intermediates observed using nuclear magnetic resonance methods for several proteins and has important implications for theoretical studies of protein folding.
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{{ABSTRACT_PUBMED_15491625}}


==About this Structure==
==About this Structure==
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYX OCA].  
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYX 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 16:58:49 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:26:29 2008''

Revision as of 11:26, 28 July 2008

File:1yyx.png

Template:STRUCTURE 1yyx

The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) at 2.8M urea

Template:ABSTRACT PUBMED 15491625

About this Structure

Full experimental information is available from OCA.

Reference

Detection and structure determination of an equilibrium unfolding intermediate of Rd-apocytochrome b562: native fold with non-native hydrophobic interactions., Feng H, Vu ND, Bai Y, J Mol Biol. 2004 Nov 5;343(5):1477-85. PMID:15491625

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