Intrinsic tryptophans of CRABPI as probes of structure and folding

Protein Science

Volumn 5, Issue 6, 1996, Pages 1108-1117

  Clark, Patricia L ^a,b   Liu, Zhi Ping ^a   Zhang, Jianhua ^a,c   Gierasch, Lila M ^b  

^a UNIVERSITY OF TEXAS AT DALLAS   (United States)

^b UNIVERSITY OF MASSACHUSETTS   (United States)

^c WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

Author keywords

aromatic charge interaction; fluorescence; near and far UV CD; retinoic acid binding protein; tryptophan

Indexed keywords

RETINOIC ACID; RETINOIC ACID BINDING PROTEIN; TRYPTOPHAN;

AMINO ACID SEQUENCE; ARTICLE; FLUORESCENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE; SPECTROSCOPY;

EID: 0029929965     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050613     Document Type: Article

References (23)

1. Banaszak L, Winter N, Xu Z, Bernlohr DA, Cowan S, Jones TA. 1994. Lipid-binding proteins: A family of fatty acid and retinoid transport proteins. Adv Protein Chem 45:89-151.
2. Cogan U, Kopelman M, Mokady S, Shinitzky M. 1976. Binding affinities of retinol and related compounds to retinol binding proteins. Eur J Biochem 65:71-78.
3. Demchenko AP. 1986. Ultraviolet spectroscopy of proteins. New York: Springer-Verlag. pp 159-166.
4. Gill SC, von Hippel PH. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Analyt Biochem 182:319-326.
5. Goldenberg DP. 1992. Mutational analysis of protein folding and stability. In: Creighton TE, ed. Protein folding. New York: W.H Freeman and Company. pp 353-355.
6. Johnson WC Jr. 1988. Secondary structure of proteins through circular dichroism spectroscopy. Annu Rev Biophys Biophys Chem 17.145-166.
7. Johnson WC Jr. 1990. Protein secondary structure and circular dichroism: A practical guide. Proteins Struct Fund Genet 7:205-214.
8. Kieywegt GJ, Bergfors T, Senn H, Motte PL, Gsell B, Shudo K, Jones TA. 1994. Crystal structure of cellular retinoic-acid-binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid. Structure 2:1241-1258.
9. Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
10. Kuwajima K, Yamaya H, Miwa S, Sugai S, Nagamura T. 1987. Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS Letters 221:115-118.
11. Kwon OH, Churchich JE. 1994. Interaction of 70-kDa heat shock cognate protein with peptide and myo-inositol monophosphatase. J Biol Chem 269:266-271.
12. Liu ZP, Rizo J, Gierasch LM. 1994, Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly β-sheet protein. Biochemistry 33:134-142.
13. Locke BC, MacInnis JM, Qian SJ, Gordon JI, Li E, Fleming GR, Yang NC. 1992. Fluorescence studies of rat cellular retinol binding protein-II produced in E. coil-An anatjsis of four tryptophan substitution mutants. Biochemistry 31:2376-2383.
14. Loewenthal R, Sancho J, Fersht AR. 1991. Fluorescence spectrum of barnase - Contributions of three tryptophan residues and a histidine-related pH dependence. Biochemistry 30:6775-6119.
15. 15N resonance assignments and secondary structure of cellular retinoic acid-binding protein with and without bound ligand. J Biomol NMR 4:741-760.
16. Ropson IJ, Gordon JI, Frieden C. 1990. Folding of a predominantly β-structure protein: Rat intestinal fatty acid binding protein. Biochemistry 29:9591-9599.
17. 19F NMR. Proc Natl Acad Sci USA 89:7222-7226.
18. Rule GS, Pratt EA, Simplaceanu V, Ho C. 1987. Nuclear magnetic resonance and molecular genetic studies of the membrane-bound D-lactate dehydrogenase of Escherichia coli. Biochemistry 26:549-556.
19. Strickland EH. 1974. Aromatic contributions to circular dichroism spectra of proteins. CAC Crit Rev Biochem 2:113-175.
20. Varley P, Gronenborn AM, Christensen H, Wingfield PT, Pain RH, Clore GM. 1993. Kinetics of folding of the all β-sheet protein interleukin-1-β. Science 260:1110-1113.
21. Vuilleumier S, Sancho J, Loewenthal R, Fersht AR. 1993. Circular dichroism studies of barnase and us mutants: Characterization of the contribution of aromatic side chains. Biochemistry 32:1030-10313.
22. Wasylewski Z, Koloczek H, Wasniowska A, Slizowska K. 1992. Red-edge excitation fluorescence measurements of several two-tryptophan-contaming proteins. Eur J Biochem 206:235-242.
23. Zhang J, Liu ZP, Jones TA, Gierasch LM, Sambrook JF. 1992. Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability. Proteins Struct Funct Genet 13:87-99.