Record Details

INCREASED EXPOSURE OF HYDROPHOBIC SURFACE IN MOLTEN GLOBULE STATE OF ALPHA-LACTALBUMIN - FLUORESCENCE AND HYDROPHOBIC PHOTOLABELING STUDIES

DSpace at IIT Bombay

View Archive Info
 
 
Field Value
 
Title INCREASED EXPOSURE OF HYDROPHOBIC SURFACE IN MOLTEN GLOBULE STATE OF ALPHA-LACTALBUMIN - FLUORESCENCE AND HYDROPHOBIC PHOTOLABELING STUDIES
 
Creator LALA, AK
KAUL, P
 
Subject compact state
protein
ion
ph
tryptophyl
vesicles
binding
fusion
nmr
 
Description The involvement of molten globule state as a distinct intermediate in the denaturation process in proteins is well documented. However, the structural characterization of such an intermediate is far from complete. We have, using fluorescence and fluorescence quenching, studied the molten globule state of bovine alpha-lactalbumin. Unlike the native state, where all the 4 tryptophans are buried in the protein, 2 tryptophans are exposed in the molten globule state. Using the hydrophobic photoactivable reagent [H-3]diazofluorene, we observe an increased hydrophobic exposure in the molten globule state. These structural characteristics conform to the current views on the molten globule state, i.e. it has similar secondary structure but a poorly defined tertiary structure. Our fluorescence studies indicate the involvement of a premolten globule state in the native to molten globule state transition. This premolten globule state exists at pH 5.0 and has a very compact structure involving increased hydrophobic interactions in the protein interior. These results are also supported by circular dichroism studies.
 
Publisher AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
 
Date 2011-07-17T04:57:24Z
2011-12-26T12:50:07Z
2011-12-27T05:36:07Z
2011-07-17T04:57:24Z
2011-12-26T12:50:07Z
2011-12-27T05:36:07Z
1992
 
Type Article
 
Identifier JOURNAL OF BIOLOGICAL CHEMISTRY, 267(28), 19914-19918
0021-9258
http://dspace.library.iitb.ac.in/xmlui/handle/10054/4620
http://hdl.handle.net/10054/4620
 
Language en