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Differential dehydration effects on globular proteins and intrinsically
disordered proteins during film formation
#MMPMID28097742
Yoneda JS
; Miles AJ
; Araujo AP
; Wallace BA
Protein Sci
2017[Apr]; 26
(4
): 718-726
PMID28097742
show ga
Globular proteins composed of different secondary structures and fold types were
examined by synchrotron radiation circular dichroism spectroscopy to determine
the effects of dehydration on their secondary structures. They exhibited only
minor changes upon removal of bulk water during film formation, contrary to
previously reported studies of proteins dehydrated by lyophilization (where
substantial loss of helical structure and gain in sheet structure was detected).
This near lack of conformational change observed for globular proteins contrasts
with intrinsically disordered proteins (IDPs) dried in the same manner: the IDPs,
which have almost completely unordered structures in solution, exhibited
increased amounts of regular (mostly helical) secondary structures when
dehydrated, suggesting formation of new intra-protein hydrogen bonds replacing
solvent-protein hydrogen bonds, in a process which may mimic interactions that
occur when IDPs bind to partner molecules. This study has thus shown that the
secondary structures of globular and intrinsically disordered proteins behave
very differently upon dehydration, and that films are a potentially useful format
for examining dehydrated soluble proteins and assessing IDPs structures.
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