We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1yyj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1yyj.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1yyj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1yyj| PDB=1yyj | SCENE= }}
{{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===
-
==Overview==
+
<!--
-
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.
 +
-->
 +
{{ABSTRACT_PUBMED_14580191}}
==About this Structure==
==About this Structure==
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYJ OCA].
+
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YYJ OCA].
==Reference==
==Reference==
Line 32: Line 36:
[[Category: Psi]]
[[Category: Psi]]
[[Category: Structural genomic]]
[[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 Tue Jul 29 06:24:07 2008''

Revision as of 03:24, 29 July 2008

Image:1yyj.png

Template:STRUCTURE 1yyj

The NMR solution structure of a redesigned apocytochrome b562:Rd-apocyt b562

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

Page seeded by OCA on Tue Jul 29 06:24:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yyj"
Personal tools