Abstract:
:We have examined the conformational behavior under various unfolding conditions of a predominantly beta-sheet protein, cellular retinoic acid binding protein (CRABP). Urea unfolding-refolding of CRABP is a highly cooperative process that can be approximated by a two-state model. Acid denaturation is also cooperative and reversible and leads to a state containing nonnative residual structure: Below pH 2.6, CRABP contains a substantially larger amount of alpha-helix than under native conditions. CRABP adopts up to 75% alpha-helix in solutions containing a high percentage of 2,2,2-trifluoroethanol. The acid-denatured state of CRABP undergoes a conformational change to a state containing predominantly beta-sheet structure upon the addition of small amounts of Na2SO4. This conformational malleability may be important for the folding mechanism of CRABP. The possible implication of nonnative alpha-helical structure in the folding of CRABP is discussed.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Liu ZP,Rizo J,Gierasch LMdoi
10.1021/bi00167a017subject
Has Abstractpub_date
1994-01-11 00:00:00pages
134-42issue
1eissn
0006-2960issn
1520-4995journal_volume
33pub_type
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