2f4k: Difference between revisions

Revision as of 13:53, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2f4k.png

Template:STRUCTURE 2f4k

Chicken villin subdomain HP-35, K65(NLE), N68H, K70(NLE), PH9Chicken villin subdomain HP-35, K65(NLE), N68H, K70(NLE), PH9

Template:ABSTRACT PUBMED 16643946

About this StructureAbout this Structure

2F4K is a Single protein structure. Full crystallographic information is available from OCA.

ReferenceReference

Sub-microsecond protein folding., Kubelka J, Chiu TK, Davies DR, Eaton WA, Hofrichter J, J Mol Biol. 2006 Jun 9;359(3):546-53. Epub 2006 Mar 31. PMID:16643946

Page seeded by OCA on Mon Jul 28 13:53:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2f4k.gif|left|200px]]
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 {{STRUCTURE_2f4k|  PDB=2f4k  |  SCENE=  }}
-'''Chicken villin subdomain HP-35, K65(NLE), N68H, K70(NLE), PH9'''
+===Chicken villin subdomain HP-35, K65(NLE), N68H, K70(NLE), PH9===
-==Overview==
+<!--
-We have investigated the structure, equilibria, and folding kinetics of an engineered 35-residue subdomain of the chicken villin headpiece, an ultrafast-folding protein. Substitution of two buried lysine residues by norleucine residues stabilizes the protein by 1 kcal/mol and increases the folding rate sixfold, as measured by nanosecond laser T-jump. The folding rate at 300 K is (0.7 micros)(-1) with little or no temperature dependence, making this protein the first sub-microsecond folder, with a rate only twofold slower than the theoretically predicted speed limit. Using the 70 ns process to obtain the effective diffusion coefficient, the free energy barrier height is estimated from Kramers theory to be less than approximately 1 kcal/mol. X-ray crystallographic determination at 1A resolution shows no significant change in structure compared to the single-norleucine-substituted molecule and suggests that the increased stability is electrostatic in origin. The ultrafast folding rate, very accurate X-ray structure, and small size make this engineered villin subdomain an ideal system for simulation by atomistic molecular dynamics with explicit solvent.
+The line below this paragraph, {{ABSTRACT_PUBMED_16643946}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16643946 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16643946}}
 ==About this Structure==
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 [[Category: Kubelka, J.]]
 [[Category: Villin head group subdomain]]
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