1hyp: Difference between revisions

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

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

caption="1hyp, resolution 1.8Å" />

'''CRYSTAL STRUCTURE OF HYDROPHOBIC PROTEIN FROM SOYBEAN; A MEMBER OF A NEW CYSTINE-RICH FAMILY'''<br />

==Overview==

X-ray diffraction methods have been used to determine the structure of the, 8.3 kDa hydrophobic protein from soybean and to refine the atomic, co-ordinates to a crystallographic R-factor of 18.7% at 1.8 A resolution., The molecule is a four-helix bundle, which together with the connecting, loops and a twisted beta-strand form a spiral. The surface contains 70%, apolar atoms, and the crystal packing is dominated by hydrophobic, interactions, producing a two-dimensional sheet of protein molecules. Most, of the 59 water molecules located are involved in hydrophilic contacts and, their structural organization does not seem to be affected by the high, hydrophobicity of the molecule. From the protein fold it appears that, three of the four disulphide bridges are important for keeping the amino, and carboxyl-terminal segments in place in the native form, while the, central part of the molecule is stabilized by many hydrophobic, interactions. Although the protein function is not known, a number of, possibilities can be excluded on experimental grounds and by comparison, with other members of the family.

X-ray diffraction methods have been used to determine the structure of the 8.3 kDa hydrophobic protein from soybean and to refine the atomic co-ordinates to a crystallographic R-factor of 18.7% at 1.8 A resolution. The molecule is a four-helix bundle, which together with the connecting loops and a twisted beta-strand form a spiral. The surface contains 70% apolar atoms, and the crystal packing is dominated by hydrophobic interactions, producing a two-dimensional sheet of protein molecules. Most of the 59 water molecules located are involved in hydrophilic contacts and their structural organization does not seem to be affected by the high hydrophobicity of the molecule. From the protein fold it appears that three of the four disulphide bridges are important for keeping the amino and carboxyl-terminal segments in place in the native form, while the central part of the molecule is stabilized by many hydrophobic interactions. Although the protein function is not known, a number of possibilities can be excluded on experimental grounds and by comparison with other members of the family.

==About this Structure==

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

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

==Reference==

Line 13:

[[Category: Glycine max]]

[[Category: Single protein]]

[[Category: al., M.S.Lehmann.et.]]

[[Category: al., M S.Lehmann et.]]

[[Category: hydrophobic seed protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 16~~:55:~~04 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:14 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1hyp.gif|left|200px]]<br /><applet load="1hyp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1hyp.gif|left|200px]]<br /><applet load="1hyp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1hyp, resolution 1.8&Aring;" />
 '''CRYSTAL STRUCTURE OF HYDROPHOBIC PROTEIN FROM SOYBEAN; A MEMBER OF A NEW CYSTINE-RICH FAMILY'''<br />
 ==Overview==
-X-ray diffraction methods have been used to determine the structure of the, 8.3 kDa hydrophobic protein from soybean and to refine the atomic, co-ordinates to a crystallographic R-factor of 18.7% at 1.8 A resolution., The molecule is a four-helix bundle, which together with the connecting, loops and a twisted beta-strand form a spiral. The surface contains 70%, apolar atoms, and the crystal packing is dominated by hydrophobic, interactions, producing a two-dimensional sheet of protein molecules. Most, of the 59 water molecules located are involved in hydrophilic contacts and, their structural organization does not seem to be affected by the high, hydrophobicity of the molecule. From the protein fold it appears that, three of the four disulphide bridges are important for keeping the amino, and carboxyl-terminal segments in place in the native form, while the, central part of the molecule is stabilized by many hydrophobic, interactions. Although the protein function is not known, a number of, possibilities can be excluded on experimental grounds and by comparison, with other members of the family.
+X-ray diffraction methods have been used to determine the structure of the 8.3 kDa hydrophobic protein from soybean and to refine the atomic co-ordinates to a crystallographic R-factor of 18.7% at 1.8 A resolution. The molecule is a four-helix bundle, which together with the connecting loops and a twisted beta-strand form a spiral. The surface contains 70% apolar atoms, and the crystal packing is dominated by hydrophobic interactions, producing a two-dimensional sheet of protein molecules. Most of the 59 water molecules located are involved in hydrophilic contacts and their structural organization does not seem to be affected by the high hydrophobicity of the molecule. From the protein fold it appears that three of the four disulphide bridges are important for keeping the amino and carboxyl-terminal segments in place in the native form, while the central part of the molecule is stabilized by many hydrophobic interactions. Although the protein function is not known, a number of possibilities can be excluded on experimental grounds and by comparison with other members of the family.
 ==About this Structure==
-HYP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HYP OCA].
+HYP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYP OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Glycine max]]
 [[Category: Single protein]]
-[[Category: al., M.S.Lehmann.et.]]
+[[Category: al., M S.Lehmann et.]]
 [[Category: hydrophobic seed protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:55:04 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:14 2008''