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==Overview==

Proteins from halophiles have adapted to challenging environmental, conditions and require salt for their structure and function. How, halophilic proteins adapted to a hypersaline environment is still an, intriguing question. It is important to mimic the physiological conditions, of the archae extreme halophiles when characterizing their enzymes, including structural characterization. The NMR derived structure of, Haloferax volcanii dihydrofolate reductase in 3.5 M NaCl is presented, and, represents the first high salt structure calculated using NMR data., Structure calculations show that this protein has a solution structure, which is similar to the previously determined crystal structure with a, difference at the N terminus of beta3 and the type of beta-turn connection, beta7 and beta8.

Proteins from halophiles have adapted to challenging environmental conditions and require salt for their structure and function. How halophilic proteins adapted to a hypersaline environment is still an intriguing question. It is important to mimic the physiological conditions of the archae extreme halophiles when characterizing their enzymes, including structural characterization. The NMR derived structure of Haloferax volcanii dihydrofolate reductase in 3.5 M NaCl is presented, and represents the first high salt structure calculated using NMR data. Structure calculations show that this protein has a solution structure which is similar to the previously determined crystal structure with a difference at the N terminus of beta3 and the type of beta-turn connection beta7 and beta8.

==About this Structure==

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[[Category: oxidoreductase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:55:47 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Proteins from halophiles have adapted to challenging environmental, conditions and require salt for their structure and function. How, halophilic proteins adapted to a hypersaline environment is still an, intriguing question. It is important to mimic the physiological conditions, of the archae extreme halophiles when characterizing their enzymes, including structural characterization. The NMR derived structure of, Haloferax volcanii dihydrofolate reductase in 3.5 M NaCl is presented, and, represents the first high salt structure calculated using NMR data., Structure calculations show that this protein has a solution structure, which is similar to the previously determined crystal structure with a, difference at the N terminus of beta3 and the type of beta-turn connection, beta7 and beta8.
+Proteins from halophiles have adapted to challenging environmental conditions and require salt for their structure and function. How halophilic proteins adapted to a hypersaline environment is still an intriguing question. It is important to mimic the physiological conditions of the archae extreme halophiles when characterizing their enzymes, including structural characterization. The NMR derived structure of Haloferax volcanii dihydrofolate reductase in 3.5 M NaCl is presented, and represents the first high salt structure calculated using NMR data. Structure calculations show that this protein has a solution structure which is similar to the previously determined crystal structure with a difference at the N terminus of beta3 and the type of beta-turn connection beta7 and beta8.
 ==About this Structure==
@@ Line 20: / Line 20: @@
 [[Category: oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:45:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:55:47 2008''