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provided by a Center grant funded by
NIH/NCRR. Primary support for the subproject
and the subproject's principal investigator may
have been provided by other sources, including
other NIH sources. The Total Cost listed for thesubproject likely represents the estimatedamount of Center infrastructure utilized by thesubproject, not direct funding provided by theNCRR grant to the subproject or subproject staff.
Our understanding of many biological processes
is limited by a lack of simple, robust approaches
to obtain molecular structures. To circumventthese limitations, we must extend the size andcomplexity of the proteins of biological interest.
This may be done by chemical crosslinking.
Chemical crosslinking of proteins, or the transfer
of a chemical group to one protein, is generallyaccomplished by reaction with a cross-linking
agent such as a polyamine, disuccinimidyl
suberate (DSS), bis[sulfosuccinimidyl]suberate(BS3), or transglutaminase. These crosslinking
agents or cross-linkers are heterogenous, but
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we have shown that crosslinking proteins attheir N-termini is a useful method for resolving
protein oligomers (Drisler, JA et al., Biochemistry
42:4634, 2003;Drisler, JA et al., J. Struct. Biol.
143:193, 2004;Drisler, JA et al., Proc. Natl. Acad.
Sci. USA 100:9302, 2003), we have usedcrosslinking to develop new methods for protein
purification (Scherrer, CA et al., Methods Mol.
Biol. 198:91, 2001), and we have usedcrosslinking to derive structures and determine
the modes of action for many proteins ofbiomedical interest.Novel markers of cholestasis
reveal distinct patterns of hepatic bile salt
disposition and the cholehepatic shunting of bilesalts in rats with cholestasis. 1cdb36666d
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