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cronos0910

http://www.ncbi.nlm.nih.gov/pubmed/17892305
0 R  I5 j# S/ dCrystal structure of type 1 ribonuclease H from hyperthermophilic archaeon Sulfolobus tokodaii: role of arginine 118 and C-terminal anchoring.1 y; k9 {0 {( `' ]' n
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http://www.ncbi.nlm.nih.gov/pubmed/22185502
% b6 t6 T2 C% Y( zThermal Unfolding Of Nucleoside Hydrolases From The Hyperthermophilic Archaeon Sulfolobus Solfataricus: Role Of Disulfide Bonds3 `: g2 z, y1 _

2 ~  b* v, V7 [9 P) @http://www.ncbi.nlm.nih.gov/pubmed/16930136
# h! l! C2 I, I- {/ ?, N+ ^Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles.% z0 n' G0 f0 |3 g

( h0 u, M$ f, `1 z3 W  Shttp://www.ncbi.nlm.nih.gov/pubmed/15606771: A% g3 p8 \% a9 t7 @- u( Y
Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and assignment of disulfide bonds
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http://www.ncbi.nlm.nih.gov/pubmed/11863449' O0 V" Q0 D! a0 @
A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond.
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1 U2 h8 g# e: bhttp://www.ncbi.nlm.nih.gov/pubmed/12479408
7 E7 q5 r  ~' _0 Z  F& Z6 |2 C; tExceptional stability of a [2Fe-2S] ferredoxin from hyperthermophilic bacterium Aquifex aeolicus.
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; U. G; o* z5 i. P. E5 V& z- Chttp://www.ncbi.nlm.nih.gov/pubmed/11601981
# p* j' F" q- i; ISolution NMR characterization of the thermodynamics of the disulfide bond orientational isomerism and its effect of cluster electronic properties for the hyperthermostable three-iron cluster ferredoxin from the archaeon Pyrococcus furiosus.$ A+ \. j! I2 p2 j* {

$ H% P0 I! s* N, nhttp://www.ncbi.nlm.nih.gov/pubmed/16721657, x- t' _4 m* X7 d/ q( Z# X
Intersubunit disulfide interactions play a critical role in maintaining the thermostability of glucose-6-phosphate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus.  B9 i7 v! S$ A9 E4 `1 c

$ p  s% ?# C/ l: D6 ^8 u# O. ihttp://www.ncbi.nlm.nih.gov/pubmed/12369841* G9 V2 _8 |% Y' U1 V/ [- Z
A solution NMR molecular model for the aspartate-ligated, cubane cluster containing ferredoxin from the hyperthermophilic archeaon Pyrococcus furiosus
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/ \) W4 d4 d5 Nhttp://www.ncbi.nlm.nih.gov/pubmed/10387062
$ n) W$ n& \0 A) ?Secondary structure extensions in Pyrococcus furiosus ferredoxin destabilize the disulfide bond relative to that in other hyperthermostable ferredoxins. Global consequences for the disulfide orientational heterogeneity% I& A1 @/ W. C& j) ~6 a

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