4hb1
From Proteopedia
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[[Image:4hb1.jpg|left|200px]] | [[Image:4hb1.jpg|left|200px]] | ||
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| - | + | {{STRUCTURE_4hb1| PDB=4hb1 | SCENE= }} | |
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'''A DESIGNED FOUR HELIX BUNDLE PROTEIN.''' | '''A DESIGNED FOUR HELIX BUNDLE PROTEIN.''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HB1 OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/9406555 9406555] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9406555 9406555] | ||
| - | [[Category: Protein complex]] | ||
| - | [[Category: Synthetic construct]] | ||
[[Category: Laporte, S L.]] | [[Category: Laporte, S L.]] | ||
[[Category: Miercke, L J.W.]] | [[Category: Miercke, L J.W.]] | ||
[[Category: Schafmeister, C E.]] | [[Category: Schafmeister, C E.]] | ||
[[Category: Stroud, R M.]] | [[Category: Stroud, R M.]] | ||
| - | [[Category: | + | [[Category: Designed helical bundle]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:25:05 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:25, 4 May 2008
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
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 Sun May 4 22:25:05 2008
