1qgm: Difference between revisions

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[[Image:1qgm.jpg|left|200px]]<br /><applet load="1qgm" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1qgm.jpg|left|200px]]<br /><applet load="1qgm" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1qgm" />

'''THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.'''<br />

==Overview==

Upon air oxidation, a peptide corresponding to the 30-residue N-terminal, subdomain of carp granulin-1 spontaneously formed the disulfide pairing, observed in the native protein. Structural characterization using NMR, showed the presence of a defined secondary structure within this peptide., The chemical shifts for most of the alphaCH protons of the peptide and the, protein are very similar, and the observed NOE contacts of the peptide, strongly resemble those in the protein. A structure calculation of the, peptide using NOE distance constraints indicates that the peptide fragment, adopts the same conformation as formed within the native protein. The, 30-residue N-terminal peptide of carp granulin-1 is the first example of, an independently folded stack of two beta-hairpins reinforced by two, interhairpin disulfide bonds. Two key areas of the structure show a, clustering of hydrophobic residues that may account for its exceptional, conformational stability.

Upon air oxidation, a peptide corresponding to the 30-residue N-terminal subdomain of carp granulin-1 spontaneously formed the disulfide pairing observed in the native protein. Structural characterization using NMR showed the presence of a defined secondary structure within this peptide. The chemical shifts for most of the alphaCH protons of the peptide and the protein are very similar, and the observed NOE contacts of the peptide strongly resemble those in the protein. A structure calculation of the peptide using NOE distance constraints indicates that the peptide fragment adopts the same conformation as formed within the native protein. The 30-residue N-terminal peptide of carp granulin-1 is the first example of an independently folded stack of two beta-hairpins reinforced by two interhairpin disulfide bonds. Two key areas of the structure show a clustering of hydrophobic residues that may account for its exceptional conformational stability.

==About this Structure==

1QGM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1QGM OCA].

1QGM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGM OCA].

==Reference==

Line 13:

[[Category: Single protein]]

[[Category: Ni, F.]]

[[Category: Vranken, W.F.]]

[[Category: Vranken, W F.]]

[[Category: Xu, P.]]

[[Category: beta-hairpin stack]]

[[Category: conformational stability]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 00:40:~~30 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:22 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1qgm.jpg|left|200px]]<br /><applet load="1qgm" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1qgm.jpg|left|200px]]<br /><applet load="1qgm" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1qgm" />
 '''THE SOLUTION STRUCTURE OF A 30 RESIDUE AMINO-TERMINAL DOMAIN OF THE CARP GRANULIN-1 PROTEIN.'''<br />
 ==Overview==
-Upon air oxidation, a peptide corresponding to the 30-residue N-terminal, subdomain of carp granulin-1 spontaneously formed the disulfide pairing, observed in the native protein. Structural characterization using NMR, showed the presence of a defined secondary structure within this peptide., The chemical shifts for most of the alphaCH protons of the peptide and the, protein are very similar, and the observed NOE contacts of the peptide, strongly resemble those in the protein. A structure calculation of the, peptide using NOE distance constraints indicates that the peptide fragment, adopts the same conformation as formed within the native protein. The, 30-residue N-terminal peptide of carp granulin-1 is the first example of, an independently folded stack of two beta-hairpins reinforced by two, interhairpin disulfide bonds. Two key areas of the structure show a, clustering of hydrophobic residues that may account for its exceptional, conformational stability.
+Upon air oxidation, a peptide corresponding to the 30-residue N-terminal subdomain of carp granulin-1 spontaneously formed the disulfide pairing observed in the native protein. Structural characterization using NMR showed the presence of a defined secondary structure within this peptide. The chemical shifts for most of the alphaCH protons of the peptide and the protein are very similar, and the observed NOE contacts of the peptide strongly resemble those in the protein. A structure calculation of the peptide using NOE distance constraints indicates that the peptide fragment adopts the same conformation as formed within the native protein. The 30-residue N-terminal peptide of carp granulin-1 is the first example of an independently folded stack of two beta-hairpins reinforced by two interhairpin disulfide bonds. Two key areas of the structure show a clustering of hydrophobic residues that may account for its exceptional conformational stability.
 ==About this Structure==
-QGM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QGM OCA].
+QGM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGM OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Single protein]]
 [[Category: Ni, F.]]
-[[Category: Vranken, W.F.]]
+[[Category: Vranken, W F.]]
 [[Category: Xu, P.]]
 [[Category: beta-hairpin stack]]
 [[Category: conformational stability]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:40:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:22 2008''