View source for 1em7

[[Image:1em7.jpg|left|200px]]<br /><applet load="1em7" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="1em7, resolution 2.0&Aring;" />
'''HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G'''<br />

==Overview==
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==
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EM7 OCA]. 

==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10933505 10933505]
[[Category: Single protein]]
[[Category: Streptococcus sp.]]
[[Category: Marinescu, A.M.]]
[[Category: Mayo, S.L.]]
[[Category: Strop, P.]]
[[Category: helix dipole interaction]]
[[Category: helix propensity]]
[[Category: protein design]]
[[Category: protein g]]

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