1yzc

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(New page: 200px<br /><applet load="1yzc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yzc" /> '''The solution structure of a redesigned apocy...)
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[[Image:1yzc.gif|left|200px]]<br /><applet load="1yzc" size="350" color="white" frame="true" align="right" spinBox="true"
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'''The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N- and a part of the C-terminal helices unfolded'''<br />
'''The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N- and a part of the C-terminal helices unfolded'''<br />
==Overview==
==Overview==
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Using native-state hydrogen-exchange-directed protein engineering and, multidimensional NMR, we determined the high-resolution structure (rms, deviation, 1.1 angstroms) for an intermediate of the four-helix bundle, protein: Rd-apocytochrome b562. The intermediate has the N-terminal helix, and a part of the C-terminal helix unfolded. In earlier studies, we also, solved the structures of two other folding intermediates for the same, protein: one with the N-terminal helix alone unfolded and the other with a, reorganized hydrophobic core. Together, these structures provide a, description of a protein folding pathway with multiple intermediates at, atomic resolution. The two general features for the intermediates are (i), native-like backbone topology and (ii) nonnative side-chain interactions., These results have implications for important issues in protein folding, studies, including large-scale conformation search, -value analysis, and, computer simulations.
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Using native-state hydrogen-exchange-directed protein engineering and multidimensional NMR, we determined the high-resolution structure (rms deviation, 1.1 angstroms) for an intermediate of the four-helix bundle protein: Rd-apocytochrome b562. The intermediate has the N-terminal helix and a part of the C-terminal helix unfolded. In earlier studies, we also solved the structures of two other folding intermediates for the same protein: one with the N-terminal helix alone unfolded and the other with a reorganized hydrophobic core. Together, these structures provide a description of a protein folding pathway with multiple intermediates at atomic resolution. The two general features for the intermediates are (i) native-like backbone topology and (ii) nonnative side-chain interactions. These results have implications for important issues in protein folding studies, including large-scale conformation search, -value analysis, and computer simulations.
==About this Structure==
==About this Structure==
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1YZC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YZC OCA].
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1YZC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YZC OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
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[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: Bai, Y.]]
[[Category: Bai, Y.]]
[[Category: Feng, H.]]
[[Category: Feng, H.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:40:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:10:38 2008''

Revision as of 14:10, 21 February 2008


1yzc

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The solution structure of a redesigned apocytochrome B562 (Rd-apocyt b562) with the N- and a part of the C-terminal helices unfolded

Overview

Using native-state hydrogen-exchange-directed protein engineering and multidimensional NMR, we determined the high-resolution structure (rms deviation, 1.1 angstroms) for an intermediate of the four-helix bundle protein: Rd-apocytochrome b562. The intermediate has the N-terminal helix and a part of the C-terminal helix unfolded. In earlier studies, we also solved the structures of two other folding intermediates for the same protein: one with the N-terminal helix alone unfolded and the other with a reorganized hydrophobic core. Together, these structures provide a description of a protein folding pathway with multiple intermediates at atomic resolution. The two general features for the intermediates are (i) native-like backbone topology and (ii) nonnative side-chain interactions. These results have implications for important issues in protein folding studies, including large-scale conformation search, -value analysis, and computer simulations.

About this Structure

1YZC is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A protein folding pathway with multiple folding intermediates at atomic resolution., Feng H, Zhou Z, Bai Y, Proc Natl Acad Sci U S A. 2005 Apr 5;102(14):5026-31. Epub 2005 Mar 25. PMID:15793003

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