1lyy: Difference between revisions

Line 4:

==Overview==

Tissue deposition of soluble proteins as amyloid fibrils underlies a range, of fatal diseases. The two naturally occurring human lysozyme variants are, both amyloidogenic, and are shown here to be unstable. They aggregate to, form amyloid fibrils with transformation of the mainly helical native, fold, observed in crystal structures, to the amyloid fibril cross-beta, fold. Biophysical studies suggest that partly folded intermediates are, involved in fibrillogenesis, and this may be relevant to amyloidosis, generally.

Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-beta fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.

==Disease==

Line 17:

[[Category: Lysozyme]]

[[Category: Single protein]]

[[Category: Blake, C.C.F.]]

[[Category: Blake, C C.F.]]

[[Category: Sunde, M.]]

[[Category: 4-glycan-hydrolase]]

Line 24:

[[Category: hydrolase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:21:20 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:50 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-Tissue deposition of soluble proteins as amyloid fibrils underlies a range, of fatal diseases. The two naturally occurring human lysozyme variants are, both amyloidogenic, and are shown here to be unstable. They aggregate to, form amyloid fibrils with transformation of the mainly helical native, fold, observed in crystal structures, to the amyloid fibril cross-beta, fold. Biophysical studies suggest that partly folded intermediates are, involved in fibrillogenesis, and this may be relevant to amyloidosis, generally.
+Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-beta fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.
 ==Disease==
@@ Line 17: / Line 17: @@
 [[Category: Lysozyme]]
 [[Category: Single protein]]
-[[Category: Blake, C.C.F.]]
+[[Category: Blake, C C.F.]]
 [[Category: Sunde, M.]]
 [[Category: 4-glycan-hydrolase]]
@@ Line 24: / Line 24: @@
 [[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:21:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:50 2008''