Turn scanning by site-directed mutagenesis: Application to the protein folding problem using the intestinal fatty acid binding protein

Protein Science

Volumn 7, Issue 8, 1998, Pages 1821-1828

  Kim, Keehyuk ^a   Frieden, Carl ^b  

^a Woosong University   (South Korea)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Fatty acid binding; Turn mutations; Sheet protein folding and stability

Indexed keywords

FATTY ACID BINDING PROTEIN; GLYCINE; MUTANT PROTEIN; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; DENATURATION; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN LIPID INTERACTION; PROTEIN MODIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

EID: 0032469297     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070818     Document Type: Article

References (21)

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. 1H exchange. Biochemistry 36:2278-2290.
3. Hodsdon ME, Ponder JW, Cistola DP. 1996. The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: Application of a novel distance geometry algorithm. J Mol Biol 264:585-602.
4. Hynes TR, Kautz RA, Goodman MA, Gill JF, Fox RO. 1989. Transfer of a beta-turn structure to a new protein context. Nature 339:73-16.
5. Kim K, Cistola DP, Frieden C. 1996. Intestinal fatty acid-binding protein: The structure and stability of a helix-less variant. Biochemistry 35:7553-7558.
6. Kim K, Ramanathan R, Frieden C. 1997. Intestinal fatty acid binding protein: A specific residue in one turn appears to stabilize the native structure and be responsible for slow refolding. Protein Sci 6:364-372.
7. Kraulis P. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein stucture. J Appl Crystallog 24:946-950.
8. Kurian E, Kirk WR, Prendergast FG. 1996. Affinity of fatty acid for rat intestinal fatty acid binding protein: Further examination. Biochemistry 35:3865-3874.
9. Minor DL Jr, Kim PS. 1994a. Context is a major determinant of beta-sheet propensity. Nature 371:264-267.
10. Minor DL Jr, Kim PS. 1994b. Measurement of the beta-sheet-forming propensities of amino acids. Nature 367:660-663.
11. Plaxco KW, Simons ST, Baker D. 1998. Contact order, transition state placement and the refolding rates of single domain proteins. J Mol Biol 277:985-994.
12. Ramirez-Alvarado M, Blanco FJ, Serrano L. 1996. De novo design and structural analysis of a model beta-hairpin peptide system. Nat Struct Biol 3:604-612.
13. Richieri GV, Ogata RT, Kleinfeld AM. 1996. Kinetics of fatty acid interactions with fatty acid binding proteins from adipocyte, heart, and intestine. J Biol Chem 271:11291-11300.
14. Ropson U, Frieden C. 1992. Dynamic NMR spectral analysis and protein folding: Identification of a highly populated folding intermediate of rat intestinal fatty acid-binding protein by 19F NMR. Proc Natl Acad Sci USA 59:7222-7226.
15. Ropson IJ, Gordon JI, Frieden C. 1990. Folding of a predominantly beta-structure protein: Rat intestinal fatty acid binding protein. Biochemistry 29:9591-9599.
16. Rose GD, Gierasch LM, Smith JA. 1985. Turns in peptides and proteins. Adv Protein Chem 37:1-109.
17. Sacchettini JC, Gordon JI. 1993. Rat intestinal fatty acid binding protein. A model system for analyzing the forces that can bind fatty acids to proteins. [Review]. J Biol Chem 268:18399-18402.
18. Sacchettini JC, Scapin G, Gopaul D, Gordon JI. 1992. Refinement of the structure of Escherichia-coli-derived rat intestinal fatty-acid binding-protein with bound oleate to 1.75-angstrom resolution: Correlation with the structures of the apoprotein and the protein with bound palmitate. J Biol Chem 267:23534-23545.
19. Santoro MM, Bolen DW. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry 27:8063-8068.
20. Scapin G, Gordon JI, Sacchettini JC. 1992. Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2 Å resolution. J Biol Chem 267:4253-4269.
21. Serrano L, Matouschek A, Fersht AR. 1992. The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. J Mol Biol 224:805-818.