1e0q

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(New page: 200px<br /><applet load="1e0q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e0q" /> '''MUTANT PEPTIDE FROM THE FIRST N-TERMINAL 17 ...)
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'''MUTANT PEPTIDE FROM THE FIRST N-TERMINAL 17 AMINO-ACID OF UBIQUITIN'''<br />
'''MUTANT PEPTIDE FROM THE FIRST N-TERMINAL 17 AMINO-ACID OF UBIQUITIN'''<br />
==Overview==
==Overview==
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The formation of the N-terminal beta-hairpin of ubiquitin is thought to be, an early event in the folding of this small protein. Previously, we have, shown that a peptide corresponding to residues 1-17 of ubiquitin folds, autonomously and is likely to have a native-like hairpin register. To, investigate the causes of the stability of this fold, we have made, mutations in the amino acids at the apex of the turn. We find that in a, peptide where Thr9 is replaced by Asp, U(1-17)T9D, the native conformation, is stabilized with respect to the wild-type sequence, so much so that we, are able to characterize the structure of the mutant peptide fully by NMR, spectroscopy. The data indicate that U(1-17)T9D peptide does indeed form a, hairpin with a native-like register and a type I turn with a G1, beta-bulge, as in the full-length protein. The reason for the greater, stability of the U(1-17)T9D mutant remains uncertain, but there are, nuclear Overhauser effects between the side chains of Asp9 and Lys 11, which may indicate that a charge-charge interaction between these residues, is responsible.
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The formation of the N-terminal beta-hairpin of ubiquitin is thought to be an early event in the folding of this small protein. Previously, we have shown that a peptide corresponding to residues 1-17 of ubiquitin folds autonomously and is likely to have a native-like hairpin register. To investigate the causes of the stability of this fold, we have made mutations in the amino acids at the apex of the turn. We find that in a peptide where Thr9 is replaced by Asp, U(1-17)T9D, the native conformation is stabilized with respect to the wild-type sequence, so much so that we are able to characterize the structure of the mutant peptide fully by NMR spectroscopy. The data indicate that U(1-17)T9D peptide does indeed form a hairpin with a native-like register and a type I turn with a G1 beta-bulge, as in the full-length protein. The reason for the greater stability of the U(1-17)T9D mutant remains uncertain, but there are nuclear Overhauser effects between the side chains of Asp9 and Lys 11, which may indicate that a charge-charge interaction between these residues is responsible.
==About this Structure==
==About this Structure==
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1E0Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E0Q OCA].
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1E0Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E0Q OCA].
==Reference==
==Reference==
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chen, P.Y.]]
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[[Category: Chen, P Y.]]
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[[Category: Evans, P.A.]]
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[[Category: Evans, P A.]]
[[Category: Raine, A.]]
[[Category: Raine, A.]]
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[[Category: Williams, D.H.]]
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[[Category: Williams, D H.]]
[[Category: Zerella, R.]]
[[Category: Zerella, R.]]
[[Category: hairpin]]
[[Category: hairpin]]
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[[Category: ubiquitin]]
[[Category: ubiquitin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:43:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:31 2008''

Revision as of 10:22, 21 February 2008

Image:1e0q.gif

1e0q

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MUTANT PEPTIDE FROM THE FIRST N-TERMINAL 17 AMINO-ACID OF UBIQUITIN

Overview

The formation of the N-terminal beta-hairpin of ubiquitin is thought to be an early event in the folding of this small protein. Previously, we have shown that a peptide corresponding to residues 1-17 of ubiquitin folds autonomously and is likely to have a native-like hairpin register. To investigate the causes of the stability of this fold, we have made mutations in the amino acids at the apex of the turn. We find that in a peptide where Thr9 is replaced by Asp, U(1-17)T9D, the native conformation is stabilized with respect to the wild-type sequence, so much so that we are able to characterize the structure of the mutant peptide fully by NMR spectroscopy. The data indicate that U(1-17)T9D peptide does indeed form a hairpin with a native-like register and a type I turn with a G1 beta-bulge, as in the full-length protein. The reason for the greater stability of the U(1-17)T9D mutant remains uncertain, but there are nuclear Overhauser effects between the side chains of Asp9 and Lys 11, which may indicate that a charge-charge interaction between these residues is responsible.

About this Structure

1E0Q is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structural characterization of a mutant peptide derived from ubiquitin: implications for protein folding., Zerella R, Chen PY, Evans PA, Raine A, Williams DH, Protein Sci. 2000 Nov;9(11):2142-50. PMID:11152124

Page seeded by OCA on Thu Feb 21 12:22:31 2008

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