4hb1
From Proteopedia
(New page: 200px<br /><applet load="4hb1" size="350" color="white" frame="true" align="right" spinBox="true" caption="4hb1, resolution 2.9Å" /> '''A DESIGNED FOUR HELIX...) |
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==Overview== | ==Overview== | ||
| - | A 108 amino acid protein was designed and constructed from a reduced | + | A 108 amino acid protein was designed and constructed from a reduced alphabet of seven amino acids. The 2.9 A resolution X-ray crystal structure confirms that the protein is a four helix bundle, as it was designed to be. Hydrogen/deuterium exchange experiments reveal buried amide protons with protection factors in excess of 1 x 10(6) in the range characteristic of well protected protons in functional folded proteins (10(3)-10(8)) rather than protons in rapid exchange (0-10(2)). The protein is monomeric at 1 mM, the concentration at which the exchange experiments were undertaken, indicating that the exchange factors are due to a unique stable tertiary structure fold, and not due to any higher order quaternary structure. Thermodynamic analysis provides an estimate of the free energy of folding of -9.3 kcal mole-1 at 25 degrees C, consistent with the free energy of folding derived from the protection factors of the most protected protons, indicating that global unfolding is required for exchange of the most protected protons. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
| - | [[Category: Laporte, S | + | [[Category: Laporte, S L.]] |
| - | [[Category: Miercke, L | + | [[Category: Miercke, L J.W.]] |
| - | [[Category: Schafmeister, C | + | [[Category: Schafmeister, C E.]] |
| - | [[Category: Stroud, R | + | [[Category: Stroud, R M.]] |
[[Category: UNX]] | [[Category: UNX]] | ||
[[Category: designed helical bundle]] | [[Category: designed helical bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:35 2008'' |
Revision as of 17:13, 21 February 2008
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A DESIGNED FOUR HELIX BUNDLE PROTEIN.
Overview
A 108 amino acid protein was designed and constructed from a reduced alphabet of seven amino acids. The 2.9 A resolution X-ray crystal structure confirms that the protein is a four helix bundle, as it was designed to be. Hydrogen/deuterium exchange experiments reveal buried amide protons with protection factors in excess of 1 x 10(6) in the range characteristic of well protected protons in functional folded proteins (10(3)-10(8)) rather than protons in rapid exchange (0-10(2)). The protein is monomeric at 1 mM, the concentration at which the exchange experiments were undertaken, indicating that the exchange factors are due to a unique stable tertiary structure fold, and not due to any higher order quaternary structure. Thermodynamic analysis provides an estimate of the free energy of folding of -9.3 kcal mole-1 at 25 degrees C, consistent with the free energy of folding derived from the protection factors of the most protected protons, indicating that global unfolding is required for exchange of the most protected protons.
About this Structure
4HB1 is a Protein complex structure of sequences from Synthetic construct with as ligand. Full crystallographic information is available from OCA.
Reference
A designed four helix bundle protein with native-like structure., Schafmeister CE, LaPorte SL, Miercke LJ, Stroud RM, Nat Struct Biol. 1997 Dec;4(12):1039-46. PMID:9406555
Page seeded by OCA on Thu Feb 21 19:13:35 2008
