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cronos0910

http://www.ncbi.nlm.nih.gov/pubmed/17892305' D+ p0 D% E) v
Crystal structure of type 1 ribonuclease H from hyperthermophilic archaeon Sulfolobus tokodaii: role of arginine 118 and C-terminal anchoring.6 S& ?+ y) |" c

0 g& r8 U: k" ^$ F& D* c( Qhttp://www.ncbi.nlm.nih.gov/pubmed/221855025 f3 J  P$ _% B
Thermal Unfolding Of Nucleoside Hydrolases From The Hyperthermophilic Archaeon Sulfolobus Solfataricus: Role Of Disulfide Bonds
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" l- C5 p7 K3 n7 [# T2 y9 Y, Khttp://www.ncbi.nlm.nih.gov/pubmed/16930136% d  k% Q9 e7 }& n
Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles.
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http://www.ncbi.nlm.nih.gov/pubmed/15606771
/ c7 O0 I, n+ J0 EMethylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus. Mechanism of the reaction and assignment of disulfide bonds
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/ s# w# Y5 H9 p% W, L' c5 C$ |" Z4 khttp://www.ncbi.nlm.nih.gov/pubmed/11863449
0 d2 p' r! j3 @A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond.
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http://www.ncbi.nlm.nih.gov/pubmed/12479408
4 `1 A4 b; u  |) d8 e9 WExceptional stability of a [2Fe-2S] ferredoxin from hyperthermophilic bacterium Aquifex aeolicus.9 \6 B. s  U8 F, u/ B

/ C3 a  x2 u5 ^! I, l6 r' `* Rhttp://www.ncbi.nlm.nih.gov/pubmed/11601981
" V& G/ k& R9 l4 ?+ r/ A, M* MSolution 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.2 n' Q" \& Y% }0 n

) V: m4 A; K! }' \8 J+ P& g9 v% ghttp://www.ncbi.nlm.nih.gov/pubmed/16721657% w& j+ ~8 ?' L: j. j2 {9 x
Intersubunit disulfide interactions play a critical role in maintaining the thermostability of glucose-6-phosphate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus.; l8 f# A7 ~, v$ _+ f
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http://www.ncbi.nlm.nih.gov/pubmed/12369841
$ ~3 Y& s4 Q& Z1 LA solution NMR molecular model for the aspartate-ligated, cubane cluster containing ferredoxin from the hyperthermophilic archeaon Pyrococcus furiosus
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) L* h0 d+ w+ G2 i, ihttp://www.ncbi.nlm.nih.gov/pubmed/10387062; O+ v% q- Q  B
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$ P2 C6 i; w7 W$ @2 c& t3 E

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