NDLI: Intrinsic tryptophans of CRABPI as probes of structure and folding.

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Intrinsic tryptophans of CRABPI as probes of structure and folding.

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Intrinsic tryptophans of CRABPI as probes of structure and folding.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Clark, P. L. Liu, Z. P. Gierasch, L. M. Zhang, J.
Description	Country affiliation: United States Author Affiliation: Clark PL ( Molecular Biophysics Graduate Program, University of Texas Southwestern Medical Center at Dallas 75235, USA.)
Abstract	The native state fluorescence and CD spectra of the predominantly beta-sheet cellular retinoic acid-binding protein I (CRABPI) include contributions from its three tryptophan residues and are influenced by the positions of these residues in the three-dimensional structure. Using a combination of spectroscopic approaches and single Trp-mutants of CRABPI, we have deconvoluted these spectra and uncovered several features that have aided in our analysis of the development of structure in the folding pathway of CRABPI. The emission spectrum of native CRABPI is dominated by Trp 7. Trp 109 is fluorescence-silent due to its interaction with the guanidino group of Arg 111. Although the far-UV CD spectrum of CRABPI is largely determined by the protein's secondary structure, aromatic clustering around Trp 87 and the aromatic-charge interaction between Arg 111 and Trp 109 give rise to a characteristic feature in the CD spectrum at 228 nm. The near-UV CD bands of CRABPI arise largely from additive contributions of the three tryptophan residues. Trp 7 and Trp 87 give a negative CD band at 275 nm. The near-UV CD band from Trp 109 is positive and shifted to longer wavelengths (to 302 nm) due to the charge-aromatic interaction between Arg 111 and Trp 109. Our deconvolution of the equilibrium spectra have been used to interpret kinetic folding experiments monitored by stopped-flow fluorescence. These dynamic experiments suggest the early evolution of a well-populated, hydrophobically collapsed intermediate, which undergoes global rearrangement to form the fully folded structure. The results presented here suggest several additional strategies for dissecting the folding pathway of CRABPI.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	6
Volume Number	5
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1996-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Receptors, Retinoic Acid Chemistry Tryptophan Circular Dichroism Fluorescence Gene Expression Point Mutation Genetics Protein Conformation Protein Denaturation Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Isolation & Purification Recombinant Proteins Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Titrimetry Tretinoin Urea Comparative Study Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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