2bkg: Difference between revisions

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==Overview==

Consensus-designed ankyrin repeat (AR) proteins are thermodynamically very, stable. The structural analysis of the designed AR protein E3_5 revealed, that this stability is due to a regular fold with highly conserved, structural motifs and H-bonding networks. However, the designed AR protein, E3_19 exhibits a significantly lower stability than E3_5 (9.6 vs. 14.8, kcal/mol), despite 88% sequence identity. To investigate the structural, correlations of this stability difference between E3_5 and E3_19, we, determined the crystal structure of E3_19 at 1.9 A resolution. E3_19 as, well has a regular AR domain fold with the characteristic H-bonding, patterns. All structural features of the E3_5 and E3_19 molecules appear, to be virtually identical (RMSD(Calpha) approximately 0.7 A). However, clear differences are observed in the surface charge distribution of the, two AR proteins. E3_19 features clusters of charged residues and more, exposed hydrophobic residues than E3_5. The atomic coordinates of E3_19, have been deposited in the Protein Data Bank. PDB ID: 2BKG.

Consensus-designed ankyrin repeat (AR) proteins are thermodynamically very stable. The structural analysis of the designed AR protein E3_5 revealed that this stability is due to a regular fold with highly conserved structural motifs and H-bonding networks. However, the designed AR protein E3_19 exhibits a significantly lower stability than E3_5 (9.6 vs. 14.8 kcal/mol), despite 88% sequence identity. To investigate the structural correlations of this stability difference between E3_5 and E3_19, we determined the crystal structure of E3_19 at 1.9 A resolution. E3_19 as well has a regular AR domain fold with the characteristic H-bonding patterns. All structural features of the E3_5 and E3_19 molecules appear to be virtually identical (RMSD(Calpha) approximately 0.7 A). However, clear differences are observed in the surface charge distribution of the two AR proteins. E3_19 features clusters of charged residues and more exposed hydrophobic residues than E3_5. The atomic coordinates of E3_19 have been deposited in the Protein Data Bank. PDB ID: 2BKG.

==About this Structure==

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[[Category: ]]

[[Category: Single protein]]

[[Category: Binz, H.K.]]

[[Category: Binz, H K.]]

[[Category: Grutter, M.G.]]

[[Category: Grutter, M G.]]

[[Category: Kohl, A.]]

[[Category: Pluckthun, A.]]

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[[Category: protein stability]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Consensus-designed ankyrin repeat (AR) proteins are thermodynamically very, stable. The structural analysis of the designed AR protein E3_5 revealed, that this stability is due to a regular fold with highly conserved, structural motifs and H-bonding networks. However, the designed AR protein, E3_19 exhibits a significantly lower stability than E3_5 (9.6 vs. 14.8, kcal/mol), despite 88% sequence identity. To investigate the structural, correlations of this stability difference between E3_5 and E3_19, we, determined the crystal structure of E3_19 at 1.9 A resolution. E3_19 as, well has a regular AR domain fold with the characteristic H-bonding, patterns. All structural features of the E3_5 and E3_19 molecules appear, to be virtually identical (RMSD(Calpha) approximately 0.7 A). However, clear differences are observed in the surface charge distribution of the, two AR proteins. E3_19 features clusters of charged residues and more, exposed hydrophobic residues than E3_5. The atomic coordinates of E3_19, have been deposited in the Protein Data Bank. PDB ID: 2BKG.
+Consensus-designed ankyrin repeat (AR) proteins are thermodynamically very stable. The structural analysis of the designed AR protein E3_5 revealed that this stability is due to a regular fold with highly conserved structural motifs and H-bonding networks. However, the designed AR protein E3_19 exhibits a significantly lower stability than E3_5 (9.6 vs. 14.8 kcal/mol), despite 88% sequence identity. To investigate the structural correlations of this stability difference between E3_5 and E3_19, we determined the crystal structure of E3_19 at 1.9 A resolution. E3_19 as well has a regular AR domain fold with the characteristic H-bonding patterns. All structural features of the E3_5 and E3_19 molecules appear to be virtually identical (RMSD(Calpha) approximately 0.7 A). However, clear differences are observed in the surface charge distribution of the two AR proteins. E3_19 features clusters of charged residues and more exposed hydrophobic residues than E3_5. The atomic coordinates of E3_19 have been deposited in the Protein Data Bank. PDB ID: 2BKG.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: ]]
 [[Category: Single protein]]
-[[Category: Binz, H.K.]]
+[[Category: Binz, H K.]]
-[[Category: Grutter, M.G.]]
+[[Category: Grutter, M G.]]
 [[Category: Kohl, A.]]
 [[Category: Pluckthun, A.]]
@@ Line 22: / Line 22: @@
 [[Category: protein stability]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:26:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:44 2008''