1em7: Difference between revisions
New page: left|200px<br /><applet load="1em7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1em7, resolution 2.0Å" /> '''HELIX VARIANT OF THE ... |
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[[Image:1em7.jpg|left|200px]]<br /><applet load="1em7" size=" | [[Image:1em7.jpg|left|200px]]<br /><applet load="1em7" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1em7, resolution 2.0Å" /> | caption="1em7, resolution 2.0Å" /> | ||
'''HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G'''<br /> | '''HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G'''<br /> | ||
==Overview== | ==Overview== | ||
Six helix surface positions of protein G (Gbeta1) were redesigned using a | Six helix surface positions of protein G (Gbeta1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gbeta1m2. Gbeta1m2 is well folded with a circular dichroism spectrum nearly identical to that of Gbeta1, and a melting temperature of 91 degrees C, approximately 6 degrees C higher than that of Gbeta1. The crystal structure of Gbeta1m2 was solved to 2.0 A resolution by molecular replacement. The absence of hydrogen bond or salt bridge interactions between the designed residues in Gbeta1m2 suggests that the increased stability of Gbeta1m2 is due to increased helix propensity and more favorable helix dipole interactions. | ||
==About this Structure== | ==About this Structure== | ||
1EM7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full crystallographic information is available from [http:// | 1EM7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EM7 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptococcus sp.]] | [[Category: Streptococcus sp.]] | ||
[[Category: Marinescu, A | [[Category: Marinescu, A M.]] | ||
[[Category: Mayo, S | [[Category: Mayo, S L.]] | ||
[[Category: Strop, P.]] | [[Category: Strop, P.]] | ||
[[Category: helix dipole interaction]] | [[Category: helix dipole interaction]] | ||
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[[Category: protein g]] | [[Category: protein g]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:17 2008'' | ||
Revision as of 13:29, 21 February 2008
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HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G
OverviewOverview
Six helix surface positions of protein G (Gbeta1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gbeta1m2. Gbeta1m2 is well folded with a circular dichroism spectrum nearly identical to that of Gbeta1, and a melting temperature of 91 degrees C, approximately 6 degrees C higher than that of Gbeta1. The crystal structure of Gbeta1m2 was solved to 2.0 A resolution by molecular replacement. The absence of hydrogen bond or salt bridge interactions between the designed residues in Gbeta1m2 suggests that the increased stability of Gbeta1m2 is due to increased helix propensity and more favorable helix dipole interactions.
About this StructureAbout this Structure
1EM7 is a Single protein structure of sequence from Streptococcus sp.. Full crystallographic information is available from OCA.
ReferenceReference
Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design., Strop P, Marinescu AM, Mayo SL, Protein Sci. 2000 Jul;9(7):1391-4. PMID:10933505
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