1. DNA-like double helix formed by peptide nucleic acid P. Wittung, Peter Nielsen, O. Buchart, M. Egholm, B. Norden, Nature, 1994, 368, 561-563.   
 2. Interactions between DNA Molecules Bound to RecA Filament, effects of base complementary  P. Wittung, M. Takahashi, B. Norden, J. Biol. Chem., 1994, 269, 5799-5803.
 3. Spectroscopic observation of renaturation between polynucleotides interacting with RecA in presence of ATP hydrolysis P. Wittung, M. Takahashi, B. Norden, Eur. J. Biochem., 1994, 224, 39-45.
 4. The cupredoxin fold is found in the soluble CuA and CyoA domains of two terminal oxidases P. Wittung, B. Kallebrink, B. Malmstrom, FEBS Letters, 1994, 349, 286-288.
 5. Structure - Activity Studies of the binding of modified PNA to DNA B. Hyrup, M. Egholm, P. Nielsen, P. Wittung, B. Norden, O. Buchardt, J. Am. Chem. Soc., 1994, 116, 7964-7970.
 6. Crystallization and Preliminary Diffraction Studies of E. coli Lysyl tRNA synthetase (LysU) S. Onesti, M.-E. Theoclitou, P. Wittung, A. Miller, P. Plateau, S. Blanquet, P. Brick. J. Mol. Biol., 1994, 243, 123-125.
 7. Absorption flattening in the optical spectra of liposome trapped substances P. Wittung, J. Kajanus, M. Kubista, B. Malmstrom, FEBS Letters, 1994, 352, 37-40.
 8. Interactions of DNA binding ligands with PNA-DNA hybrids P. Wittung, S. Kim, P. Nielsen, O. Buchardt & B. Norden, Nucleic Acid Research, 1994, 22, 5371-5377.
 9. Secondary Structure of RecA in Solution The effects of cofactor, DNA and ionic conditions P. Wittung, B. Norden, M. Takahashi, Eur. J. Biochem., 1995, 228, 149-154.
10. Triplet state quenching in complexes of Zn-Cyt c and cyt. oxidase or its CuA domain: evidence that CuA is primary site of electron entry P. Brezezinski, M. Sundahl, P. Adelroth, M. Wilson, B. El-Agez, P. Wittung, B. Malmstrom, Biophys. Chem., 1995, 54, 191-197.
11. The CuA center of cytochrome c oxidase: electronic structure of models compared to the properties of CuA domains S. Larsson, B. Kallebrink, P. Wittung, B. Malmstrom, Pro. Nat. Acad. Sci. USA, 1995, 92, 7167-7171.
12. Phospholipid membrane permeability of peptide nucleic acid P. Wittung, J. Kajanus, K. Edwards, P. Nielsen, B. Norden, B. Malmstrom, FEBS Letters, 1995, 365, 27-29.
13. Fluorescence-detected interactions of oligonucleotides with RecA complexes P. Wittung, M. Funk, B. Jernstrom, B. Norden, M. Takahashi, FEBS Letters, 1995, 368, 64-68.
14. Induced chirality in PNA-PNA duplexes P. Wittung, M. Eriksson, R. Lyng, P. Nielsen, B. Norden, J. Am. Chem. Soc, 1995, 117, 10167-10173.
15. Evidence for elongation of the helical pitch of the RecA filament upon ATP and ADP binding using small angle neutron scattering C. Ellouze, M. Takahashi, P. Wittung, K. Mortensen, M. Schnarr, B. Norden, Eur. J. Biochem., 1995, 233, 579-583.
16. Electron transfer studies with the CuA domain of Thermus thermophilus cytochrome ba3 C. Slutter, R. Langen, D. Sanders, S. Lawrence, P. Wittung, A. DiBilio, M. Hill, J. Fee, J. Richards, J. Winkler, B. Malmstrom, Inorganica Chimica Acta, 1996, 243, 1-5.
17. PNA-Peptide Chimerae T. Koch, M. Naesby, P. Wittung, M. Jorgensen, C. Larsson, O. Buchardt, C. Stanely, B. Norden, P. Nielsen, H. Orum, Tetrahed. Lett., 1995, 36, 6933-6936.
18. A water-soluble, reconbinant CuA-domain of the Cytochrome ba3 subunit II from Thermus thermophilus C. Slutter, D. Sanders, P. Wittung, B. Malmstrom, R. Aasa, J. Richards, H.B. Gray, J. Fee, Biochemistry 1996, 35, 3387-3395.
19. Ionic Effects on the Stability and Conformation of Peptide Nucleic Acid (PNA) complexes S. Tomac, M. Sarkar, T. Ratilainen, P. Wittung, P. Nielsen, B. Norden, A. Graslund, J. Am. Chem. Soc, 1996, 118, 5544-5552.
20. Direct Observation of Strand Invasion by Peptide Nucleic Acid (PNA) into Double-Stranded DNA P. Wittung, P. Nielsen, B. Norden, J. Am. Chem. Soc, 1996, 118, 7049-7054.
21. Redox-linked conformational changes in cytochrome c oxidase P. Wittung, B.Malmstrom, FEBS Letters, 1996, 388, 47-49.
22. Second site RecA-interactions: lack of identical recognition P. Wittung, R. Bazemore, M. Takahashi, B. Norden, C. Radding, Biochemistry, 1996, 35, 15349-15355.
23. Characterisation of stress protein LysU. Enzymatic synthesis of diadenosine 5’,5’’’-P1,P4-tetraphosphate (Ap4A) analogues by LysU M-E. Theoclitou, P. Wittung, A. Hindley, T. El-Thaher, A.D. Miller, J. Chem. Soc., Perkin Trans. 1996, 1, 2009-2017.
24. Recognition of double-stranded DNA by Peptide Nucleic Acid P.Wittung, P. Nielsen, B. NordÈn, Nucleotides & Nucleosides, 1997, 16, 5-6, 599-602.
25. Thermochemical and kinetic evidence for nucleobase dependent RecA-DNA interactions P. Wittung, C. Ellouze, F. Maraboeuf, M. Takahashi, B. Norden, Eur. J. .Biochem., 1997, 245, 3, 715-719.
26. Observation of a PNA-PNA-PNA triplex P.Wittung, P. Nielsen, B. Norden J. Am. Chem. Soc., 1997, 119, 3189-3190.
27. Effects of folding on metalloprotein active site J. Winkler, P. Wittung-Stafshede, J. Leckner, B. Malmstrom, H. Gray, Proc. Natl. Acad. Sci. USA, 1997, 94, 4246-4249.
28. The effects of redox state on the folding free energy of azurin J. Leckner, P.Wittung, N. Bonander, B. Malmstrom, G. Karlsson, J. Biol. Inorg. Chem., 1997, 2, 368-371.
29. The effect of the metal ion on the folding energetics of azurin: a comparison of the native, zinc and apoprotein J. Leckner, N. Bonander, P. Wittung-Stafshede, B. Malmstrom, G. Karlsson, BBA Proteins and Enzymology, 1997, 1342, 19-27.
30. PNAs with a conformationally constrained chiral cyclohexyl derived backbone P. Lagriffoule, P. Wittung, K. Jensen, M. Eriksson, B. Norden, O. Buchardt, P. Nielsen, Chem. Eur. J., 1997, 3, 912-919.
31. Extended DNA-recognition repertoire of PNA P.Wittung, P. Nielsen, B. Norden Biochemistry, 1997, 36, 7973-7979.
32. PNA recognition of double-stranded DNA P. Wittung-Stafshede, in Structure, Mobility, Interaction and Expression of Biological Macromololecules (Ed:s Sarma and Sarma) Adenine Press 1998, pp 133-137.
33. Rapid formation of a four helix bundle. Cytochrome b562 folding triggered by electron transfer P. Wittung-Stafshede, H.B. Gray, J.Winkler, J. Am. Chem. Soc., 1997, 119, 9562-9563.
34. A stable, molten-globule-like cytochrome c P. Wittung-Stafshede, BBA-Proteins and Enzymology, 1998, 1382, 324-332.
35. The effect of redox state on the folding free energy of a thermostable electron-transfer metallo protein: the CuA domain of cytochrome oxidase from thermus thermophilus P. Wittung-Stafshede, B. Malmstrom, D. Sanders, J. Fee, J. Winkler, H.B. Gray, Biochemistry 1998, 37, 3172-3177.
36. Folding of deoxy myoglobin triggered by electron transfer P. Wittung-Stafshede, B.G. Malmstrom, J. Winkler, H.B. Gray, J. Phys. Chem, 1998, 102, 5599-5601.
37. Reduction potentials of blue and purple copper proteins in their unfolded states: a closer look at the protein rack P. Wittung-Stafshede, M Hill, E. Gomez, A. DiBilio, G. Karlsson, J. Leckner, J. Winkler, H. Gray, B. Malmstrom, J. Biol. Inorg. Chem, 1998, 3, 367-370.
38. Base-orientation of second DNA in RecA-DNA filaments: analysis by combination of LD and SANS in flow-oriented samples B. Norden, P. Wittung-Stafshede, H.K. Kim, C. Ellouze, K. Mortensen, M. Takahashi, J. Biol. Chem, 1998, 273, 15682-15686.
39. Protein folding triggered by electron transfer J Telford, P. Wittung-Stafshede, H.B. Gray, J R Winkler, Acc. Chem. Res, 1998, 31, 755-763.
40. High-potential intermediate states of blue and purple copper proteins P. Wittung-Stafshede, E. Gomez, A Robinson, R.Villhermosa, G. Karlsson, J. Leckner, D. Sanders, J. Fee J. Winkler, H.B. Gray, B. Malmstrom, M. Hill, BBA-Proteins and Enzymology, 1998, 1388, 437-443.
41. The L2 loop peptide of RecA stiffens and restricts base-motion of ssDNA like intact protein T Selmane, P Wittung-Stafshede, F Maraboeuf, O Voloshin, B Norden, D Camerini-Otero, M Takahashi, FEBS Letters, 1999, 446, 30-34.
42. Thermodynamic and kinetic analysis of RecA-DNA interactions for understanding of the recognition of homologous DNA F. Maraboeuf, P. Wittung-Stafshede, C. Ellouze, B. Norden, M. Takahashi in Biocalorimetry (Ed:s J.E. Ladbury and B.Z. Chowdhry) Wiley and Sons, 1998.
43. Peptide Nucleic Acids  P Wittung-Stafshede, B Norden in Encyclopedia of Molecular Biology (Ed Thomas Creighton), 2000, 1801-1808.
44. Peptide Nucleic Acids Derived from N-(N-methylaminoethyl)glycine. Synthesis, Hybridisation and Structural Properties G Haaima, H Rasmussen, G Schmidt, D Jensen, J Sandholm Kastrup, P Wittung-Stafshede, B Nordén, O Buchardt, P Nielsen, New J. Chem. 1999, 23, 833-840.
45. X-ray absorption spectroscopy of unfolded copper(I) azurin S. DeBeer, P Wittung-Stafshede, J Leckner, G Karlsson, J Winkler, HB Gray, BG Malmstrom, E. Solomon, B. Hedman, K. Hodgson, Inorg. Chim. Acta, 2000, 297, 278-282.
46. Cytochrome b562 folding triggered by electron transfer. Approaching the speed-limit for formation of a four-helix-bundle P Wittung-Stafshede, J Lee, J Winkler, HB Gray, Proc. Natl. Acad. Sci. USA, 1999, 96, 6587-6590. (Featured in Chem. & Eng. News)

Research Publications (Tulane Faculty Member):

47. Effects of protein folding on metalloprotein redox-active sites; electron-transfer properties of blue and purple copper proteins B Malmstrom, P Wittung-Stafshede, Coord. Chem. Rev, 1999, 185/186, 127-140.
48. Electron-transfer triggered time-resolved far-UV circular dichroism studies of cytochrome c folding dynamics E Chen, P Wittung-Stafshede, D Kliger, J. Am. Chem. Soc. 1999, 121, 3811-3817.
49. Equilibrium unfolding of a small low-potential cytochrome, cytochrome c553 from Desulfovibrio vulgaris P Wittung-Stafshede, Prot. Sci., 1999, 8, 1523-1529.
50. In vitro membrane penetration of modified peptide nucleic acid M Ardhammar, P Nielsen, B Norden, B Malmstrom, P Wittung-Stafshede, Biomolec. Struct. Dyn. 1999, 17(1), 33-40.
51. Effect of redox state on unfolding energetics of heme proteins P Wittung-Stafshede, BBA-Proteins and Enzymology, 1999, 1432, 401-405.
52. Detection of point mutations in DNA by quartz-crystal biosensor P Wittung-Stafshede, M Rodahl, B Kasemo, P Nielsen, B Norden Colloids & Surfaces A, 2000, 174, 269-273.
53. Stability and folding of hyperthermophilic ferredoxin from the archaeon A. Ambivalens P Wittung-Stafshede, CM Gomez, M Teixeira, J. Inorg. Biochem, 2000, 78, 35-41.
54. Effect of an organic cofactor on equilibrium unfolding of flavodoxin D Apiyo, J Guidry, P Wittung-Stafshede, BBA-Proteins and Enzymology, 2000, 1479, 214-224.
55. Stability determines folding rate of four-helix-bundle protein J Guidry, P Wittung-Stafshede, Arch. Biochem. Biophys. 2000, 378, 1, 190-191.
56. Folding and unfolding of horse metmyoglobin: effect of the heme group C. Mocszygemba, J Guidry, P Wittung-Stafshede, FEBS Letters, 2000, 470, 203-206.
57. Cytochrome c553, a small heme protein that lacks misligation in its unfolded state, folds with rapid two-state kinetics J Guidry, P Wittung-Stafshede, J. Mol. Biol., 2000, 301, 769-773.
58. Copper triggered b-hairpin formation. Initiation site for azurin folding? I Pozdnyakova, J Guidry, P Wittung-Stafshede, J. Am. Chem. Soc., 2000, 122, 6337-6338. (Featured in Chem. & Eng. News)
59. Reversible unfolding of human co-chaperonin protein cpn10 , J Guidry, C. Mocszygemba, K. Steede, S. Landry, P Wittung-Stafshede, Protein Science, 2000, 9, 2109-2117. (Featured in Chem. & Eng. News)
60.Probing copper ligands in denatured Pseudomonas aeruginosa azurin: Unfolding His117Gly and His46Gly mutants. I Pozdnyakova, J Guidry, P Wittung-Stafshede, J. Biol. Inorg. Chem, 2001, 6, 182-188.
61.  The formation speed of cyt c553 is not dependent on the nature of the unfolded state. Susanne Griffin, Jesse Guidry, Pernilla Wittung-Stafshede, Arch. Biochem. Biophys. 2001, 389, 150-152.
62.  Copper stabilizes azurin by decreasing the unfolding rate. I Pozdnyakova, J Guidry, P Wittung-Stafshede, Arch. Biochem. Biophys. 2001, 390, 146-148.
63. Equilibrium unfolding of dimeric desulfoferredoxin involves monomeric intermediate. D Apiyo, K. Jones, J Guidry, P Wittung-Stafshede, Biochemistry, 2001, 40, 4940-4948.
64. High stability of a ferredoxin from the hyperthermophilic archaeon Acidianus ambivalens: Involvement of electrostatic interactions and cofactors C Moczygemba, J Guidry, K Jones, C Gomes, M Teixeira, P Wittung-Stafshede, Protein Science, 2001, 10, 1539-1548.
65. Hybridization of 2’-modified mixed-sequence oligonucleotides: Thermodynamic and kinetic studies A Sabahi, J Guidry, G Inamati, M Manoharan, P Wittung-Stafshede, Nucleic Acid Res., 2001, 29, 2163-2170.
66. Biological relevance of metal binding before protein folding I Pozdnyakova, P Wittung-Stafshede, J. Am. Chem. Soc., 2001, 123, 10135-10136. (Featured in Chem. & Eng. News)
67. Formation of a linear [3Fe-4S] cluster in a seven-iron ferredoxin triggered by polypeptide unfolding K Jones, C Gomes, H Huber, M Teixeira, P Wittung-Stafshede, J. Biol. Inorg. Chem, 2002 7, 357-362.
68. Unfolding the unique c-type heme protein, Chlamydomonas reinhardtii cytochrome f: Stability exhibits remarkable redox dependence A Sabahi, P Wittung-Stafshede, BBA-Proteins and Enzymology, 2002, 1596, 163-171.
69. Copper binding before polypeptide folding speeds up formation of active (holo) Pseudomonas aeruginosa azurin I Pozdnyakova, P Wittung-Stafshede, Biochemistry, 2001, 2001, 40, 13728-13733.
70. Characterization of surface antigen from Lyme disease spirochete Borrelia burgdorferi K Jones, J.Guidry, P Wittung-Stafshede, Biochem Biophys Res Comm, 2001, 289, 389-394.
71. Role of cofactors in protein folding P. Wittung-Stafshede, Acc. Chem. Res., 2002, 35, 201-208.
72.  A hyperthermophilic plant-type [2Fe-2S] ferredoxin from Aquifex aeolicus is stabilized by a disulfide bond J Meyer, M Clay, M Johnson, A Stubna, E Munck, C Higgins, P Wittung-Stafshede, Biochemistry, 2002, 41, 3096-3108.
73. Cavities in b-barrel affect unfolding but not refolding speed: studies of point mutated apo-azurins. I Pozdnyakova, J Guidry, P Wittung-Stafshede, Biophys. Journal, 2002, 82, 2645-2651.
74. Presence of the cofactor speeds up folding of Desulfovibrio desurfuricans flavodoxin D Apiyo, P Wittung-Stafshede, Protein Sci., 2002, 11, 1129-1135.
75. Internal water chain in cytochrome f contributes to protein stability S Griffin., A Vitello, P Wittung-Stafshede, 2002, Arch. Biochem. Biophys. 404, 335-337.
76. Correlation between helical content and antigenicity in a conserved immunodominant region of VlsE, the antigenic variation molecule of Borrelia burgdorferi K Jones, J Guidry, K Phillippi, P Wittung-Stafshede, M Philipp, 2003, J. Infectious Disease, in press.
77. A ferredoxin from the thermohalophilic bacterium Rhodothermus marinus M Periera, K Jones, M Campos, R Louro, P Wittung-Stafshede, M Teixeira, BBA-Proteins and Enzymology, 2002, 1601, 1-8.
78. Low stability for monomeric human chaperonin protein 10: Inter-protein interactions contribute majority of oligomer stability J Guidry, P Wittung-Stafshede, 2002, Arch. Biochem. Biophys. 405, 280-282.
79. Intelligent “three-in-one” device for genetic-drug delivery J Smith, J Guidry, P Wittung-Stafshede, Prot. Pep. Letters, 2003, 10, 1-7.
80. Exceptional stability of a [2Fe-2S] ferredoxin from hyperthermophilic bacterium Aquifex aeolicus C Higgins, J Meyer, P Wittung-Stafshede, BBA-Proteins and Enzymology, 2002, 1599, 82-89.
81. If Space is Provided, Bulky Modification on the Rim of Azurin's b-barrel Results in Folded Protein I Pozdnyakova, P Wittung-Stafshede FEBS Letters, 2002, 531, 209-214.
82. An Isc-type extremely thermostable [2Fe-2S] ferredoxin from Aquifex aeolicus G Mitou, C Higgins, P Wittung-Stafshede, RC Conover, AD Smith, MK Johnson, J Gaillard, A Stubna, E Münck, J Meyer, Biochemistry, 2003, 42(5): 1354-1364.
83. Substrate capture in Hsp70 coupled by Hsp40 to ATP hydrolysis SJ Landry, BE Horne, J Guidry, P Wittung-Stafshede, Biochemistry, 2003, 42(17): 4937-4944.
84. The largest protein observed to fold by two-state kinetic mechanism does not obey contact-order correlation K Jones, P Wittung-Stafshede, J. Am. Chem Soc. 2003, 125, 9606-9607. (News Feature in Chem. & Eng. News)
85. Approaching the Speed Limit for Greek Key b-barrel Formation: Transition-state Movement Tunes Folding Rate of Zinc-substituted Azurin I Pozdnyakova, P Wittung-Stafshede, Biochem. Biphys. Acta, 2003, 1651, 1-4.
86. Can cofactor-binding sites in proteins be flexible? Desulfovibrio desulfuricans flavodoxin binds FMN dimer, BK Muralidhara, P Wittung-Stafshede, Biochemistry, 2003, 42, 13074-13080.
87. High thermal and chemical stability of Thermus thermophilus seven-iron ferredoxin: linear clusters form at high pH upon polypeptide unfolding S Griffin, C Higgins, T Soulimane P Wittung-Stafshede, Eur. J. Biochem. 2003, 270, 4736-4743.
88. Probing the Interface in a Human Co-Chaperonin Heptamer: Keystone Residue for Tertiary and Quaternary Structure Identified, J Guidry, K Maskos, S Landry P Wittung-Stafshede, BMC Biochemistry, 2003, 4:14.
89. Methionine-121 coordination determines metal specificity in unfolded Pseudomonas aeruginosa azurin: it is third metal ligand in CuII but not ZnII complex, J Marks, I Pozdnyakova, J Guidry, P Wittung-Stafshede, J. Biol. Inorg. Chem, 2004, 9, 281-288.

90. How do cofactors modulate protein folding? C Higgins, BK Muralidhara, P Wittung-Stafshede Protein Peptide Letters (Special Issue), 2005, 12, 165-170.
91. Monomer topology defines folding speed of heptamer N Baskos, J Guidry, P Wittung-Stafshede, Protein Science 2004, 13, 1317-1321.
92. First characterization of co-chaperonin protein 10 from hyper-thermophilic Aquifex aeolicus J Guidry, P Wittung-Stafshede, Biochem. Biophys. Res. Comm. 2004, 317, 176-180.
93. Slow unfolding explains high stability of thermostable ferredoxins: Common mechanism governing thermostability? P Wittung-Stafshede, Biochim Biophys Acta 2004, 1700, 1-4.
94. Formation of linear three-iron clusters in Aquifex aeolicus two-iron ferredoxins: effect of protein-unfolding speed C Higgins, P Wittung-Stafshede, Arch. Biochem. Biophys. 2004, 427, 154-163.
95. Thermal Unfolding of Apo and Holo Desulfovibrio desulfuricans Flavodoxin: Cofactor Stabilizes Native-Like Intermediate BK Muralidhara, P Wittung-Stafshede, Biochemistry 2004, 43, 12855-12864.
96. Role of cofactors in the folding of blue-copper protein azurin P. Wittung-Stafshede, Inorg. Chem. 2004, 43, 7926-7933.
97. Thermodynamics and kinetics of FMN Binding to Desulfovibrio desulfuricans Flavodoxin: Hidden intermediates at low denaturant concentrations BK Muralidhara, P Wittung-Stafshede, Biochem. Biophys. Acta 2005, 1747, 239-250.
98. Protein folding: defining a standard set of experimental conditions and a preliminary kinetic data set for two-state proteins Maxwell, K.L., Wildes, D., Zarrine-Afsar, A., de los Rios, M.A., Brown,A.G., Friel, C.T,Hedberg, L., Horng, J-C., Bona, D., Miller, E.J.,Valle-Blisle, A., Main, E.R.G., Bemporad, F., Qiu, L., Teilum, K., Vu,N.-D., Edwards, A.M., Ruczinski, I., Poulsen, F.M., Kragelund, B.B.,Michnick, S.W., Chiti, F., Bai, Y., Hagen, S.J., Serrano, L., Oliveberg,M., Raleigh, D.P., Wittung-Stafshede, P., Radford, S.E., Jackson, S.E.,Sosnick, T.R., Marqusee, S., Davidson, A.R., Plaxco, K.W. Prot Sci. 2005, 14, 602-616.
99. Role of structural determinants in folding of a sandwich like protein C. Wilson, P Wittung-Stafshede, Proc. Natl. Acad. Sci. USA, 2005, 102, 3984-3987. (Featured in Chem. & Eng. News)
100. Effect of Inorganic Phosphate on FMN Binding and Loop Flexibility in Desulfovibrio desulfuricans Apo-Flavodoxin B.K. Muralidhara, M Chen, J Ma, P Wittung-Stafshede J. Mol. Biol. 2005, 349, 87-97.  
101.  Snapshots of a dynamic folding nucleus in zinc-substituted Pseudomonas aeruginosa azurin CJ Wilson, P Wittung-Stafshede, Biochemistry, 2005, 44(30); 10054-10062.
102. Interface Mutation in Heptameric Co-Chaperonin Protein 10 Destabilizes Subunits but not Interfaces C Brown, J Liao, P Wittung-Stafshede, Arch. Biochem. Biphys. 2005, 439, 175-183.
103.  Unique Complex Between Bacterial Azurin and Tumor-Suppressor Protein p53 D Apiyo, P Wittung-Stafshede, Biochem. Biophys. Res. Comm. 2005, 332, 965-968.
104. The experimental folding landscape of monomeric lactose repressor, a large two-domain protein, involves two kinetic intermediates. C. Wilson, P. Das, Matthews KS, Clementi C. P Wittung-Stafshede, Proc. Natl. Acad. Sci. USA, 2005, 102(41):14563-8. (Featured in news eg. NSF home page, Rice News, Kemivarlden, Chalmers Magasin)
105. Characterization of the folding landscape of monomeric lactose repressor: quantitative comparison of theory and experiment  P. Das, C. Wilson, Fossati G, Wittung-Stafshede P, Matthews KS, Clementi C., Proc. Natl. Acad. Sci. USA, 2005,102(41):14569-74. (Featured in news eg. NSF home page, Rice News, Kemivarlden, Chalmers Magasin)
106.  Role of cofactors in metalloprotein folding C. Wilson, D. Apiyo, P Wittung-Stafshede, 2005, Quartenary Reviews of Biophysics, 37(3-4):285-314.
107. Dissecting homo-heptamer thermodynamics by isothermal titration calorimetry: entropy-driven assembly of co-chaperonin protein 10, K Luke, D Apiyo, P Wittung-Stafshede, 2005, Prot Sci.,  89(5):3332-6.
108.  Role of unique peptide tail in hyper-thermostable Aquifex aeolicus co-chaperonin protein 10 K Luke, D Apiyo, P Wittung-Stafshede, 2005, Biochemistry, 44(44):14385-95.
109. Protein folding: on the precision of experimentally determined phi-values MA. De Los Rios, B.K. Muralidhara, D Wildes, TR Sosnick, S Marqusee, P Wittung-Stafshede, K Plaxco I Ruczincski Prot Sci. 2006, in press.
110.  Unfolding of heptameric co-chaperonin protein follows “fly-casting” mechanism: Observation of transient nonnative heptamer M Perham, M Chen, J Ma, P Wittung-Stafshede, J Am Chem Soc, 2005, Web Release as ASAP Article November 2.
111. Solvation of the folding-transition state in Pseudomonas aeruginosa azurin is modulated by metal CJ Wilson, D Apiyo, P Wittung-Stafshede, Prot. Sci, 2006, in press.    

 1. RNA P. Wittung, B. Norden, Swedish National Encyclopedia, 1994.
 2. PNA Framtidens och urtidens molekyl  P Wittung Kemisk Tidskrift  Journal of Swedish Chemical Society, 1995, 10, 24-29.
 3. En forskare berattar (A researcher explains) P. Wittung in "Liv i Utveckling, Natura, Biologi 3" Liber, Stockholm, 1997, pp 88-89 (9th grade biology book).
 4. Genetiska lakemedel  snart mojliga  P. Wittung-Stafshede, Kemisk Tidskrift (Journal of the Swedish Chemical Society), 1998, 5, 35-39.
 5. Genetic drugs - when will it come to the drugstore? P. Wittung-Stafshede, Science 1998, 281, 657-658.
 6. Web Alert Protein Folding P. Wittung-Stafshede, Chem. Biol. 2000, 7(3), R74.
 7. Chalmerister gaskar i Florida P. Wittung-Stafshede, Chalmers Magasin, 2001, issue 3.