1z6w: Difference between revisions

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[[Image:1z6w.gif|left|200px]]<br />

[[Image:1z6w.gif|left|200px]]<br /><applet load="1z6w" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1z6w" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1z6w" />

'''Human Lactoferricin'''<br />

==Overview==

Lactoferricins are highly basic bioactive peptides that are released in, the stomach through proteolytic cleavage of various lactoferrin proteins., Here we have determined the solution structure of human lactoferricin, (LfcinH) by conventional two-dimensional nuclear magnetic resonance, methods in both aqueous solution and a membrane mimetic solvent. Unlike, the 25-residue bovine lactoferricin (LfcinB), which adopts a somewhat, distorted antiparallel beta sheet, the longer LfcinH peptide shows a, helical content from Gln14 to Lys29 in the membrane mimetic solvent but a, nonexistent beta-sheet character in either the N- or C-terminal regions of, the peptide. The helical characteristic of the LfcinH peptide resembles, the conformation that this region adopts in the crystal structure of the, intact protein. The LfcinH structure determined in aqueous solution, displays a nascent helix in the form of a coiled conformation in the, region from Gln14 to Lys29. Numerous hydrophobic interactions create the, basis for the better-defined overall structure observed in the membrane, mimetic solvent. The 49-residue LfcinH peptide isolated for these studies, was found to be slightly longer than previously reported peptide, preparations and was found to have an intact peptide bond between residues, Ala11 and Val12. The distinct solution structures of LfcinH and LfcinB, represent a novel difference in the physical properties of these two, peptides, which contributes to their unique physiological activities.

Lactoferricins are highly basic bioactive peptides that are released in the stomach through proteolytic cleavage of various lactoferrin proteins. Here we have determined the solution structure of human lactoferricin (LfcinH) by conventional two-dimensional nuclear magnetic resonance methods in both aqueous solution and a membrane mimetic solvent. Unlike the 25-residue bovine lactoferricin (LfcinB), which adopts a somewhat distorted antiparallel beta sheet, the longer LfcinH peptide shows a helical content from Gln14 to Lys29 in the membrane mimetic solvent but a nonexistent beta-sheet character in either the N- or C-terminal regions of the peptide. The helical characteristic of the LfcinH peptide resembles the conformation that this region adopts in the crystal structure of the intact protein. The LfcinH structure determined in aqueous solution displays a nascent helix in the form of a coiled conformation in the region from Gln14 to Lys29. Numerous hydrophobic interactions create the basis for the better-defined overall structure observed in the membrane mimetic solvent. The 49-residue LfcinH peptide isolated for these studies was found to be slightly longer than previously reported peptide preparations and was found to have an intact peptide bond between residues Ala11 and Val12. The distinct solution structures of LfcinH and LfcinB represent a novel difference in the physical properties of these two peptides, which contributes to their unique physiological activities.

==Disease==

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==About this Structure==

1Z6W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1Z6W OCA].

1Z6W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z6W OCA].

==Reference==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Demcoe, A.R.]]

[[Category: Demcoe, A R.]]

[[Category: Gutteberg, T.J.]]

[[Category: Gutteberg, T J.]]

[[Category: Hunter, H.N.]]

[[Category: Hunter, H N.]]

[[Category: Jenssen, H.]]

[[Category: Vogel, H.J.]]

[[Category: Vogel, H J.]]

[[Category: antimicrobial peptide]]

[[Category: aqueous]]

[[Category: helical]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 ~~20:30~~:~~10 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:46 2008''

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-[[Image:1z6w.gif|left|200px]]<br />
+[[Image:1z6w.gif|left|200px]]<br /><applet load="1z6w" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1z6w" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1z6w" />
 '''Human Lactoferricin'''<br />
 ==Overview==
-Lactoferricins are highly basic bioactive peptides that are released in, the stomach through proteolytic cleavage of various lactoferrin proteins., Here we have determined the solution structure of human lactoferricin, (LfcinH) by conventional two-dimensional nuclear magnetic resonance, methods in both aqueous solution and a membrane mimetic solvent. Unlike, the 25-residue bovine lactoferricin (LfcinB), which adopts a somewhat, distorted antiparallel beta sheet, the longer LfcinH peptide shows a, helical content from Gln14 to Lys29 in the membrane mimetic solvent but a, nonexistent beta-sheet character in either the N- or C-terminal regions of, the peptide. The helical characteristic of the LfcinH peptide resembles, the conformation that this region adopts in the crystal structure of the, intact protein. The LfcinH structure determined in aqueous solution, displays a nascent helix in the form of a coiled conformation in the, region from Gln14 to Lys29. Numerous hydrophobic interactions create the, basis for the better-defined overall structure observed in the membrane, mimetic solvent. The 49-residue LfcinH peptide isolated for these studies, was found to be slightly longer than previously reported peptide, preparations and was found to have an intact peptide bond between residues, Ala11 and Val12. The distinct solution structures of LfcinH and LfcinB, represent a novel difference in the physical properties of these two, peptides, which contributes to their unique physiological activities.
+Lactoferricins are highly basic bioactive peptides that are released in the stomach through proteolytic cleavage of various lactoferrin proteins. Here we have determined the solution structure of human lactoferricin (LfcinH) by conventional two-dimensional nuclear magnetic resonance methods in both aqueous solution and a membrane mimetic solvent. Unlike the 25-residue bovine lactoferricin (LfcinB), which adopts a somewhat distorted antiparallel beta sheet, the longer LfcinH peptide shows a helical content from Gln14 to Lys29 in the membrane mimetic solvent but a nonexistent beta-sheet character in either the N- or C-terminal regions of the peptide. The helical characteristic of the LfcinH peptide resembles the conformation that this region adopts in the crystal structure of the intact protein. The LfcinH structure determined in aqueous solution displays a nascent helix in the form of a coiled conformation in the region from Gln14 to Lys29. Numerous hydrophobic interactions create the basis for the better-defined overall structure observed in the membrane mimetic solvent. The 49-residue LfcinH peptide isolated for these studies was found to be slightly longer than previously reported peptide preparations and was found to have an intact peptide bond between residues Ala11 and Val12. The distinct solution structures of LfcinH and LfcinB represent a novel difference in the physical properties of these two peptides, which contributes to their unique physiological activities.
 ==Disease==
@@ Line 11: / Line 10: @@
 ==About this Structure==
-Z6W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z6W OCA].
+Z6W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z6W OCA].
 ==Reference==
@@ Line 17: / Line 16: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Demcoe, A.R.]]
+[[Category: Demcoe, A R.]]
-[[Category: Gutteberg, T.J.]]
+[[Category: Gutteberg, T J.]]
-[[Category: Hunter, H.N.]]
+[[Category: Hunter, H N.]]
 [[Category: Jenssen, H.]]
-[[Category: Vogel, H.J.]]
+[[Category: Vogel, H J.]]
 [[Category: antimicrobial peptide]]
 [[Category: aqueous]]
 [[Category: helical]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:30:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:46 2008''