The pH-dependent tertiary structure of a designed helix-loop-helix dimer

Folding and Design

Volumn 2, Issue 5, 1997, Pages 319-330

  Dolphin, Gunnar T ^a   Baltzer, Lars ^a  

^a UNIVERSITY OF GOTHENBURG   (Sweden)

Author keywords

De novo design; Helix loop helix; Salt bridge; Tertiary structure

Indexed keywords

GTD C PROTEIN, SYNTHETIC; GTD-C PROTEIN, SYNTHETIC; GUANIDINE; HELIX LOOP HELIX PROTEIN; PEPTIDE; PROTEIN; TRYPTOPHAN;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CIRCULAR DICHROISM; DIMERIZATION; DRUG EFFECT; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN TERTIARY STRUCTURE; SPECTROFLUOROMETRY; THEORETICAL MODEL; THERMODYNAMICS;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; DIMERIZATION; GUANIDINE; HELIX-LOOP-HELIX MOTIFS; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MODELS, THEORETICAL; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TRYPTOPHAN;

EID: 0030631493     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(97)00043-6     Document Type: Article

References (26)

1. Bryson, J.W., et al., & DeGrado, W.F. (1995). Protein design: a hierarchic approach. Science 270, 935-941.
2. Johnsson, K., Allemann, R.K., Widmer, H. & Benner, S.A. (1993). Synthesis, structure and activity of artificial, rationally designed catalytic polypeptides. Nature 365, 530-532.
3. Kaumaya, P.T.P., Berndt, K.D., Heidorn, D.B., Trewhella, J., Kezdy, FJ. & Goldberg, E. (1990). Synthesis and biophysical characterization of engineered topographic immunogenic determinants with aa topology. Biochemistry 29,13-23.
4. Rabanal, F., DeGrado, W.F. & Dutton, P.L (1996). Toward the synthesis of a photosynthetic reaction center maquette: a cofacial porphyrin pair assembled between two subunits of a synthetic four-helix bundle multiheme protein. J. Am. Chem. Soc. 118,473-474.
5. Dolgikh, D.A., et al., & Ptitsyn, O.B. (1985). Compact state of a protein molecule with pronounced small-scale mobility: bovine α-lactalbumin. Eur. Biophys. 7.13,109-121.
6. Raleigh, O.P., Betz, S.F. & DeGrado, W.F. (1995). A de novo designed protein mimics the native state of natural proteins. J. Am. Chem. Soc. 117,7558-7559.
7. Dolphin, G.T., Brive, L, Johansson, G. & Baltzer, L (1996). Use of aromatic amino acids residues to restrict the dynamics in the hydrophobic core of a designed helix-loop-helix dimer. J. Am. Chem. Soc. 118, 11297-11298.
8. Brive, L, Dolphin, G.T. & Baltzer, L. (1997). Structure and function of an aromatic ensemble that restricts the dynamics of the hydrophobic core of a designed helix-loop-helix dimer. J. Am. Chem. Soc. 119, 8598-8607.
9. Struthers, M.D., Cheng, R.P. & Impeirali, B. (1996). Design of a monomeric 23-residue polypeptide with defined tertiary structure. Science 271, 342-345.
10. Betz, S.F. & DeGrado, W.F. (1996). Controlling topology and nativelike behavior of de novo-designed peptides: design and characterization of antiparallel four-stranded coiled coils. Biochemistry 35, 6955-6962.
11. Handel, T.M., Williams, S.A. & DeGrado, W.F. (1993). Metal iondependent modulation of the dynamics of a designed protein. Science 261,879-885.
12. Waldburger, C.D., Schildbach, J.F. & Sauer, R.T. (1995). Are buried salt bridges important for protein stability and conformationa! specificity? Nat. Struct. Biol. 2, 122-128.
13. Schneider, J.P., Lear, I.D. & DeGrado, W.F. (1997). A designed buried salt bridge in a heterodimeric coiled coil. J. Am. Chem. Soc. 119, 5742-5743.
14. Baltzer, L, Lundh, A.-C., Broo, K., Olofsson, S. & Ahlberg, P. (1996). Polypeptides with supersecondary structures as templates in rational catalyst design. Catalysis of self functionalization by designed helixloop-helix motifs. J. Chem. Soc. Perkin Trans. 2,1671-1676.
15. Lundh, A.-C., Broo, K. & Baltzer, L. (1997). The relationship between structure and reactivity in a designed helix-loop-helix motif. J. Chem. Soc. Perkin Trans. 2, 209-212.
16. Zhou, N.E., Kay, C.M. & Hodges, R.S. (1994). The net energetic contribution of interhelical electrostatic attractions to coiled-coil stability. Protein Eng. 7,1365-1372.
17. Cooper, T.M. & Woody, R.W. (1990). The effect of conformation on the CD of interacting helices: a theoretical study of tropomyosin. Biopolymers 30, 657-676.
18. Lakowicz, Y. (1983). Principles of Fluorecence Spectroscopy. Plenum Press, New York.
19. Steiner, R.F. & Kirby, E.P. (1969). The interaction of the ground state and excited states of indole derivatives with electron scavengers. J. Phys. Chem. 73, 4130-4135.
20. 13CO assignments of human interleukin-4 using three-dimenstional double- and triple-resonance heteronuclear magnetic resonance spectroscopy. Biochemistry 31, 4334-4346.
21. Strickland, E.H. (1974). Aromatic contributions to circular dichroism spectra of proteins. CRC Crit. Rev. Biochem. 2,113-175.
22. Semisotnov, G.V., Rodionova, N.A., Razgulyaev, O.I., Uversky, V.N., Gripas, A.F. & Gilmanshin, R.I. (1991). Study of the "molten globule" intermediate state in protein folding by hydrophobic fluorescent probe. Biopolymers 31,119-128.
23. Tanford, C. (1962). The interpretation of hydrogen ion titration curves of proteins. Adv. Protein Chem. 17, 69-161.
24. Pace, C.N. (1986). Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280.
25. DeFrancesco, R., Pastore, A., Vecchio, G. & Cortese, R. (1991). Circular dichroism study of the conformational stability of the dimerisation domain of transcription factor LFB1. Biochemistry 30,143-147.
26. Santoro, M.M. & Boten, 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.