2f4k: Difference between revisions

Revision as of 18:17, 21 February 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

2F4K is a Single protein structure of sequence from [1]. 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 Thu Feb 21 17:17:39 2008

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

OCA

@@ Line 4: / Line 4: @@
 ==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.
+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.
 ==About this Structure==
@@ Line 12: / Line 12: @@
 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16643946 16643946]
 [[Category: Single protein]]
-[[Category: Chiu, T.K.]]
+[[Category: Chiu, T K.]]
-[[Category: Davies, D.R.]]
+[[Category: Davies, D R.]]
-[[Category: Eaton, W.A.]]
+[[Category: Eaton, W A.]]
 [[Category: Hofrichter, J.]]
 [[Category: Kubelka, J.]]
 [[Category: villin head group subdomain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:27:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:17:39 2008''