An improved experimental system for determining small folding entropy changes resulting from proline to alanine substitutions

Protein Science

Volumn 14, Issue 9, 2005, Pages 2429-2435

  Street, Timothy O ^a   Bradley, Christina Marchetti ^b   Barrick, Doug ^a  

^a JOHNS HOPKINS UNIVERSITY   (United States)

^b NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

Chemical denaturation; Notch ankyrin domain; Proline substitution; Unfolding entropy

Indexed keywords

ALANINE; NOTCH RECEPTOR; PROLINE;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; DROSOPHILA; ENTROPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN VARIANT; THERMODYNAMICS;

ALANINE; AMINO ACID SUBSTITUTION; ANKYRINS; CHEMISTRY, PHYSICAL; ENTROPY; PROLINE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; RECEPTORS, NOTCH; SOLVENTS; TEMPERATURE;

EID: 24344479918     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051505705     Document Type: Article

References (12)

1. Bork, P. 1993. Hundreds of ankyrin-like repeats in functionally diverse proteins: Mobile modules that cross phyla horizontally? Proteins 17: 363-374.
2. Bradley, C.M. and Barrick, D. 2002. Limits of cooperativity in a structurally modular protein: Response of the Notch ankyrin domain to analogous alanine substitutions in each repeat. J. Mol. Biol. 324: 373-386.
3. Ferreon, J.C. and Hilser, V.J. 2003. The effect of the polyproline II (PPII) conformation on the denatured state entropy. Protein Sci. 12: 447-457.
4. Greene, R.F.J. and Pace, C.N. 1974. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin, and β-lactoglobulin. J. Biol. Chem. 249: 5388-5393.
5. Matthews, B.W., Nicholson, H., and Becktel, W.J. 1987. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. 19: 6663-6667.
6. Pace, C.N. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131: 266-280.
7. Pickett, S.D. and Sternberg, M.J. 1993. Empirical scale of side-chain conformational entropy in protein folding. J. Mol. Biol. 231: 825-839.
8. Santoro, M.M. and Bolen, D.W. 1988. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27: 8063-8068.
9. Thompson, J.D., Higgins, D.G., and Gibson, T.J. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
10. Wharton, K.A., Johansen, K.M., Xu, T., and Artavanis-Tsakonas, S. 1985. Nucleotide sequence from the neurogenic locus notch implies a gene product that shares homology with proteins containing EGF-like repeats. Cell 43: 567-581.
11. Zweifel, M.E. and Barrick, D. 2001. Studies of the ankyrin repeats of the Drosophila melanogaster Notch receptor. 2. Solution stability and cooperativity of unfolding. Biochemistry 40: 14357-14367.
12. Zweifel, M.E., Leahy, D.J., Hughson, F.M., and Barrick, D. 2003. Structure and stability of the ankyrin domain of the Drosophila Notch receptor. Protein Sci. 11: 2622-2632.