List of Publications


Sawyer, N., Gassaway, B.M., Haimovich, A.D., Isaacs, F.J., Rinehart, J., and Regan, L.
Designed Phosphoprotein Recognition in Escherichia coli.
ACS Chemical Biology, 9(11): 2502-2507. PDF

Zhou, A.Q., O'Hern, C.S., and Regan, L.
Predicting the side-chain dihedral angle distributions of nonpolar, aromatic, and polar amino acids using hard sphere models.
Proteins, 82(10): 2574-2584. PDF

Caballero, D., Määttä, J., Zhou, A.Q., Sammalkorpi, M., O'Hern, C.S., and Regan, L.
Intrinsic alpha-helical and beta-sheet conformational preferences: A computational case study of alanine.
Protein Science, 23(7): 970-980. PDF

Schlingman, D.J., Mack, A.H., Kamenetska, M., Mochrie, S.G.J., and Regan, L.
Routes to DNA accessibility: alternative pathways for nucleosome unwinding.
Biophysical Journal, 107(2): 384-392. PDF

Zhao, Q., Saro, D., Sachpatzidis, A., Singh, T.R., Schlingman, D., Zheng, X.-F., Mack, A.,
Tsai, M.-S., Mochrie, S., Regan, L., Meetei, A.R., Sung, P., and Xiong, Y.
The MHF complex senses branched DNA by binding a pair of crossover DNA duplexes.
Nature Communications, 5: 2987. PDF


Zhou, A.Q., Caballero, D., O'Hern, C.S., and Regan, L.
New Insights into the Interdependence between Amino Acid Stereochemistry and Protein Structure.
Biophysical Journal, 105(10): 2403-2411. PDF

Mack, A.H*., Schlingman, D.J.*, Kamenetska, M., Collins, R., Mochrie, S.G.J., and Regan, L.
The molecular yo-yo method: Live jump detection improves throughput of single-molecule force spectroscopy for out-of-equilibrium transitions.
Review of Scientific Instruments, 84(8): 085119. PDF

Speltz, E. and Regan, L.
White and green screening with circular polymerase extension cloning for easy and reliable cloning.
Protein Science, 22(6): 859-864. PDF

Sawyer, N.*, Speltz, E.*, and Regan, L.
NextGen protein design.
Biochemical Society Transactions, 41(5): 1131-1136. PDF

Sawyer, N.*, Chen, J.*, and Regan, L.
All Repeats Are Not Equal: A Module-Based Approach to Guide Repeat Protein Design.
Journal of Molecular Biology, 425(10): 1826-1838. PDF

Chen, J., Sawyer, N., and Regan, L.
Protein-protein interactions: General trends in the relationship between binding affinity and interfacial buried surface area.
Protein Science, 22(4): 510-151. PDF

Grove, T.Z., Regan, L., and Cortajarena, A.L.
Nanostructured functional films from engineered repeat proteins.
Journal of the Royal Society Interface, 10(83): 20130051. PDF


Mack, A.H*., Schlingman, D.J.*, Ilagan, R.P., Mochrie, S.G.J., and Regan, L.
Kinetics and thermodynamics of phenotype: Unwinding and rewinding the nucleosome.
Journal of Molecular Biology, 423(5): 687-701. PDF

Mack, A.H., Schlingman, D.J., Regan, L., and Mochrie, S.G.J.
Practical Axial Optical Trapping.
Review of Scientific Instruments, 83(10): 103106. PDF

Grove, T.Z. and Regan, L.
New materials from proteins and peptides.
Current Opinion in Structural Biology, 22(4): 451-456. PDF

Zhou, A.Q., O'Hern, C.S., and Regan, L.
The Power of Hard-Sphere Models: Explaining Side-Chain Dihedral Angle Distributions of Thr and Val.
Biophysical Journal, 102(10): 2345-2352. PDF

Liberles, D.A., Teichmann, S.A., Bahar, I., Bastolla, U., Bloom, J.,
Bornberg-Bauer, E., Colwell, L.J., de Koning, A.P.J., Dokholyan, N.V., Echave, J. et al.
The interface of protein structure, protein biophysics, and molecular evolution.
Protein Science, 21(6): 769-785. PDF

Grove, T.Z., Forster, J., Pimienta, G., Dufresne, E., and Regan, L.
A modular approach to the design of protein-based smart gels.
Biopolymers, 97(7): 508-517. PDF

De Rosa, L., Cortajarena, A.L., Romanelli, A., Regan, L., and D'Andrea, L.D.
Site-specific protein double labeling by expressed protein ligation: applications to repeat proteins.
Organic & Biomolecular Chemistry, 10(2): 273-280. PDF


Zhou, A.Q., O'Hern, C.S., and Regan, L.
Revisiting the Ramachandran plot from a new angle.
Protein Science, 20(7): 1166-1171. PDF

Zhou, A.Q., O'Hern, C.S., and Regan, L.
Reply to: Comment on "Revisiting the Ramachandran plot from a new angle".
Protein Science, 20(11): 1774-1774. PDF

Schlingman, D.J., Mack, A.H., Mochrie, S.G.J., and Regan, L.
A new method for the covalent attachment of DNA to a surface for single-molecule studies.
Colloids and Surfaces B-Biointerfaces, 83(1): 91-95. PDF

Pimienta, G., Herbert, K.M., and Regan, L.
A Compound That Inhibits the HOP-Hsp90 Complex Formation and Has Unique Killing Effects in Breast Cancer Cell Lines.
Molecular Pharmaceutics, 8(6): 2252-2261. PDF

Cortajarena, A.L. and Regan, L.
Calorimetric study of a series of designed repeat proteins: Modular structure and modular folding.
Protein Science, 20(2): 336-340. PDF

Cortajarena, A.L., Mochrie, S.G.J., and Regan, L.
Modulating repeat protein stability: The effect of individual helix stability on the collective behavior of the ensemble.
Protein Science, 20(6): 1042-1047. PDF


Yi, F., Doudevski, I., and Regan, L.
HOP is a monomer: Investigation of the oligomeric state of the co-chaperone HOP.
Protein Science, 19(1): 19-25. PDF

Kundrat, L. and Regan, L.
Identification of Residues on Hsp70 and Hsp90 Ubiquitinated by the Cochaperone CHIP.
Journal of Molecular Biology, 395(3):587-594. PDF

Kundrat, L. and Regan, L.
Balance between Folding and Degradation for Hsp90-Dependent Client Proteins: A Key Role for CHIP.
Biochemistry, 49(35): 7428-7438. PDF

Jackrel, M.E., Cortajarena, A.L., Liu, T.Y., and Regan, L.
Screening Libraries To Identify Proteins with Desired Binding Activities Using a Split-GFP Reassembly Assay.
ACS Chemical Biology, 5(6): 553-562. PDF

Ilagan, R.P., Rhoades, E., Gruber, D.F., Kao, H.-T., Pieribone, V.A., and Regan, L.
A new bright green-emitting fluorescent protein - engineered monomeric and dimeric forms.
FEBS Journal, 277(8): 1967-1978. PDF

Grove, T.Z., Osuji, C.O., Forster, J.D., Dufresne, E.R., and Regan, L.
Stimuli-Responsive Smart Gels Realized via Modular Protein Design.
Journal of the American Chemical Society, 132(40): 14024-14026. PDF

Grove, T.Z., Hands, M., and Regan, L.
Creating novel proteins by combining design and selection.
Protein Engineering Design & Selection , 23(6): 449-455. PDF

Cortajarena, A.L., Wang, J., and Regan, L.
Crystal structure of a designed tetratricopeptide repeat module in complex with its peptide ligand.
FEBS Journal, 277(4): 1058-1066. PDF

Cortajarena, A.L., Liu, T.Y., Hochstrasser, M., and Regan, L.
Designed Proteins To Modulate Cellular Networks.
ACS Chemical Biology, 5(6): 545-552. PDF

Clarke, J. and Regan, L.
Protein engineering and design: from first principles to new technologies.
Current Opinion in Structural Biology, 20(4): 480-481. PDF


Kajander, T., Sachs, J.N., Goldman, A., and Regan, L.
Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90:
computational analysis and protein engineering.
Journal of Biological Chemistry, 284(37): 25364-25374. PDF

Champion, E.A., Kundrat, L., Regan, L., and Baserga, S.J.
A structural model for the HAT domain of Utp6 incorporating bioinformatics and genetics.
Protein Engineering Design & Selection, 22(7): 431-439. PDF

Jackrel, M.E., Valverde, R., and Regan, L.
Redesign of a protein-peptide interaction: characterization and applications.
Protein Science, 18(4): 762-774. PDF

Yi, F., Zhu, P., Southall, N., Inglese, J., Austin, C.P., Zheng, W., and Regan, L.
An AlphaScreen-Based High-Throughput Screen to Identify Inhibitors of Hsp90-Cochaperone Interaction.
Journal of Biomolecular Screening, 14(3): 273-281. PDF


Yi, F. and Regan, L.
A novel class of small molecule inhibitors of Hsp90.
ACS Chemical Biology, 3(10): 645-654. PDF

Champion, E.A., Lane, B.H., Jackrel, M.E., Regan, L, and Baserga, S.J.
A direct interaction between the Utp6 half-a-tetratricopeptide repeat domain and a specific peptide in Utp21
is essential for efficient pre-rRNA processing.
Molecular and Cellular Biology, 28(21): 6547-6556. PDF

Cortajarena, A.L., Lois, G., Sherman, E., O'Hern, C.S., Regan, L, and Haran, G.
Non-random-coil behavior as a consequence of extensive PPII structure in the denatured state.
Journal of Molecular Biology, 382(1): 203-212. PDF

Grove, T.Z., Cortajarena, A.L., and Regan, L.
Ligand binding by repeat proteins: natural and designed.
Current Opinion in Structural Biology, 18(4): 507-515. PDF

Cortajarena, A.L., Mochrie, S.G., and Regan, L.
Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange.
Journal of Molecular Biology, 379(3): 617-626. PDF

Valverde, R., Edwards, L., and Regan, L.
Structure and function of KH domains.
FEBS Journal, 275(11): 2712-2726. PDF

Cortajarena, A.L., Yi, F., and Regan, L.
Designed TPR modules as novel anticancer agents.
ACS Chemical Biology, 3(3): 161-166 . PDF

Dalal, S., Canet, D., Kaiser, S.E., Dobson, C.M., and Regan, L.
Conservation of mechanism, variation of rate: folding kinetics of three homologous four-helix bundle proteins.
Protein Engineering Design & Selection, 21(3): 197-206. PDF

van Nuland, N.A., Dobson, C.M., and Regan, L.
Characterization of folding the four-helix bundle protein Rop by real-time NMR.
Protein Engineering Design & Selection, 21(3): 165-70. PDF


Valverde, R., Pozdnyakova, I., Kajander, T.,Venkatraman, J., and Regan, L.
Fragile X Mental Retardation Syndrome: Structure of the KH1-KH2 Domains of Fragile X Mental Retardation Protein.
Structure, 15(9): 1090-1098. PDF

Kajander, T., Cortajarena, A.L., Mochrie S., and Regan, L.
Structure and stability of designed TPR protein superhelices: unusual crystal packing and implications for natural TPR proteins.
Acta Crystallographica Section D: Biological Crystallography, 63: 800-811. PDF


Cheng, C.Y., Jarymowycz, V.A., Cortajarena, A.L., Regan, L., and Stone, M.J.
Repeat Motions and Backbone Flexibility in Designed Proteins with Different Numbers of Identical Consensus Tetratricopeptide Repeats.
Biochemistry, 45(39): 12175-12183. PDF

Kajander, T., Cortajarena, A.L., and Regan, L.
Consensus Design as a Tool for Engineering Repeat Proteins.
Methods in Molecular Biology, 340: 151-170. PDF

Cortajarena, A.L. and Regan, L.
Ligand binding by TPR domains.
Protein Science, 15(5): 1193-1198. PDF

Magliery T.J. and Regan, L.
Reassembled GFP: detecting protein-protein interactions and protein expression patterns.
Methods of Biochemical Analysis, 47: 391-405. PubMed


Magliery, T.J. and Regan, L.
Sequence variation in ligand binding sites in proteins.
BMC Bioinformatics, 6: 240. PDF

Wang, J., Gulich, S., Bradford, C., Ramirez-Alvarado, M., and Regan, L.
A twisted four-sheeted model for an amyloid fibril.
Structure, 13(9): 1279-88. PDF

Main, E.R., Lowe, A.R., Mochrie, S.G., Jackson, S.E., and Regan, L.
A recurring theme in protein engineering: the design, stability and folding of repeat proteins.
Current Opinion in Structural Biology, 5(4): 464-71. PDF

Kajander, T., Cortajarena, A.L., Main, E.R., Mochrie, S.G., and Regan, L.
A new folding paradigm for repeat proteins.
Journal of the American Chemical Society, 127(29): 10188-90. PDFSupplementary Information

Main, E.R., Stott, K., Jackson, S.E., and Regan, L.
Local and long-range stability in tandemly arrayed tetratricopeptide repeats.
Proceedings of the National Academy of Sciences USA, 102(16): 5721-5726. PDF

Pozdnyakova, I. and Regan L.
New insights into Fragile X syndrome. Relating genotype to phenotype at the molecular level.
FEBS Journal, 272(3): 872-878. PDF

Wilson, C.G., Kajander, T., and Regan, L.
The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold.
FEBS Journal, 272(1): 166-179. PDF

Magliery, T.J., Wilson, C.G.M., Pan, W., Mishler, D., Ghosh, I., Hamilton, A.D., and Regan L.
Detecting protein-protein interactions with a green fluorescent protein fragment reassembly trap: scope and mechanism.
Journal of the American Chemical Society, 127(1): 146-157. PDFSupplementary Information


Wilson, C.G.M., Magliery, T.J., and Regan, L.
Detecting protein-protein interactions with GFP-fragment reassembly.
Nature Methods, 1(3): 255-262. PDFSupplementary FigureSupplementary Note

Magliery, T.J. and Regan, L.
Beyond consensus: statistical free energies reveal hidden interactions in the design of a TPR motif.
Journal of Molecular Biology, 343(3): 731-745. PDFSupplementary Information

Cortajarena, A.L., Kajander, T., Pan, W., Cocco, M., and Regan, L.
Protein design to understand peptide ligand recognition by tetratricopeptide repeat proteins.
Protein Engineering Design & Selection, 17(4): 399-409. PDF

Magliery, T.J. and Regan, L.
Library approaches to biophysical problems.
European Journal of Biochemistry, 271(9):1593-1594. PDF

Magliery, T.J. and Regan, L.
Combinatorial approaches to protein stability and structure.
European Journal of Biochemistry, 271(9): 1595-1608. PDF

Magliery, T.J. and Regan, L.
A cell-based screen for function of the four-helix bundle protein Rop: a new tool for combinatorial experiments in biophysics.
Protein Engineering Design & Selection, 17(1): 77-83. PDF


D'Andrea, L.D. and Regan, L.
TPR proteins: the versatile helix.
Trends in Biochemical Sciences, 28(12): 655-662. PDF

Mayer, K.L., Earley, M.R., Gupta, S., Pichumani, K., Regan, L., and Stone, M.J.
Covariation in backbone motion throughout a small protein domain.
Nature Structural Biology, 10(11): 962-965. PDF

Main, E.R., Jackson, S.E., and Regan, L.
The folding and design of repeat proteins: reaching a consensus.
Current Opinion in Structural Biology, 13(4): 482-489. PDF

Regan, L. and Jackson, S.E.
Engineering and design. Protein design: theory and practice.
Current Opinion in Structural Biology, 13(4): 479-481. PDF

Khurana, R., Ionescu-Zanetti, C., Pope, M., Li, J., Nielson, L., Ramirez-Alvarado, M., Regan, L., Fink, A.L., Carter, S.A.
A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy.
Biophysical Journal, 85(2): 1135-1144. PDF

Main, E.R.G., Xiong, Y., Cocco, M.J., D'Andrea, L., and Regan, L.
Design of stable α-helical arrays from an idealized TPR motif.
Structure, 11(5): 497. PDF

Regan, L.
Molten globules move into action.
Proceedings of the National Academy of Sciences USA, 100(7): 3553-3554. PDF

Ramirez-Alvarado, M., Cocco, M.J., and Regan, L.
Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro.
Protein Science, 12(3): 567-576. PDF


Ramirez-Alvarado, M. and Regan, L.
Does the location of a mutation determine the ability to form amyloid fibrils?
Journal of Molecular Biology, 323(1): 17-22. PDF


Marino, S.F., Shechner, D., and Regan, L.
'Morphs' (MRFs): metal-reversible folding domains for differential IgG binding.
Chemistry & Biology, 8(12): 1221-1229. PDF

Bishop, B., Koay, D.C., Sartorelli, A.C., and Regan, L.
Reengineering granulocyte colony-stimulating factor for enhanced stability.
Journal of Biological Chemistry, 276(36): 33465-33470. PDF

Stone, M.J., Gupta, S., Snyder, N., and Regan, L.
Comparison of protein backbone entropy and beta sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
Journal of the American Chemical Society, 123(1): 185-186. PDF

Regan, L.
Engineering and design 2001: a design odyssey.
Current Opinion in Structural Biology, 11(4): 449. PDF

Regan, L.
Current genomic research: the proteins have it.
National Academy of Engineering: Sixth Annual Symposium on Frontiers of Engineering.
Washington, DC: National Academy Press. pp 54-61. PDF


Willis, M.A., Bishop, B., Regan, L., and Brunger, A.T.
Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core.
Structure, 8(12): 1319-1328. PDF

Ramirez-Alvarado, M., Merkel, J.S., and Regan, L.
A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro.
Proceedings of the National Academy of Sciences USA, 97(16): 8979-8984. PDF

Merkel, J.S. and Regan, L.
Modulating protein folding rates in vivo and in vitro by side-chain interactions
between the parallel beta strands of green fluorescent protein.
Journal of Biological Chemistry, 275(38): 29200-29206. PDF

Dalal, S. and Regan, L.
Understanding the sequence determinants of conformational switching using protein design.
Protein Science, 9(9): 1651-1659. PDF

Seewald, M.J., Pichumani, K., Stowell, C., Tibbals, B.V., Regan, L., and Stone, M.J.
The role of backbone conformational heat capacity in protein stability:
temperature dependent dynamics of the B1 domain of Streptococcal protein G.
Protein Science, 9(6): 1177-1193. PDF

Balasubramanian, S., Schneider, T., Gerstein, M., and Regan, L.
Proteomics of Mycoplasma genitalium: identification and characterization
of unannotated and atypical proteins in a small model genome.
Nucleic Acids Research, 28(16): 3075-3082. PDF

Ghosh, I., Hamilton, A.D., and Regan, L.
Antiparallel leucine zipper-directed protein reassembly:
application to the green fluorscent protein.
Journal of the American Chemical Society, 122(23): 5658-5659. PDFSupporting Information

Lurio, L.B., Lumma, D., Sandy, A.R., Borthwick, M.A., Falus, P., Mochrie, S.G.J.,
Pelletier, J.-F., Sutton, M., Regan, L., Malik, A., Stephenson, G.B.
Absence of scaling for the intermediate scattering function of a hard-sphere suspension:
static and dynamic X-ray scattering from concentrated polystyrene latex spheres.
Physical Review Letters, 84(4): 785-788. PDF


Regan, L.
Protein redesign.
Current Opinion in Structural Biology, 9(4): 494-499. PDF

Nagi, A.D., Anderson, K.S., and Regan, L.
Using loop length variants to dissect the folding pathway of a four-helix-bundle protein.
Journal of Molecular Biology, 286(1): 257-265. PDF

Merkel, J.S., Sturtevant, J.M., and Regan, L.
Sidechain interactions in parallel beta sheets: the energetics of cross-strand pairings.
Structure, 7(11): 1333-1343. PDF

Marino, S.F. and Regan, L.
Secondary ligands enhance affinity at a designed metal-binding site.
Chemistry & Biology, 6(9): 649-655. PDF

Prodromou, C., Siligardi, G., O'Brien, R., Woolfson, D.N., Regan, L.,
Panaretou, B., Ladbury, J.E., Piper, P.W., and Pearl, L.H.
Regulation of Hsp90 ATPase activity by tetratricopeptiderepeat(TPR)-domain co-chaperones.
EMBO Journal, 18(3): 754-762. PDF

Ma, Y., Cunningham, M.E., Wang, X., Ghosh, I., Regan, L., Longely, B.J.
Inhibition of spontaneous receptor phosphorylation by residues in a putatitve alpha-helix
in the KIT intracellular juxtamembrane region.
Journal of Biological Chemistry, 274(19): 13399-13402. PDF


Regan, L. and Wells, J.
Engineering and design: recent adventures in molecular design.
Current Opinion in Structural Biology, 8(4): 441-442. PDF

Klemba, M.W., Munson, M., and Regan, L.
De novo design of protein structure and function.
Proteins: Analysis and Design. ed. Angeletti, R.H. Academic Press.

Regan, L.
Proteins to order?
Structure, 6(1): 1-4. PDF

Merkel, J.S. and Regan, L.
Aromatic rescue of glycine in beta sheets.
Folding & Design, 3(6): 449-455. PDF

Farinas, E. and Regan, L.
The de novo design of a rubredoxin-like Fe site.
Protein Science, 7(9): 1939-1946. PDF


Smith, C.K. and Regan, L.
Construction and design of β-sheets.
Accounts of Chemical Research, 30(4): 153-161. PDF

Regan, L.
Engineering metal binding site in proteins.
Advances in Molecular and Cell Biology, 22: 51-80.
ed. Allewell, N. and Woodward, C. 22. Elsevier.

Regan, L.
Helix is a helix is a helix?
Proceedings of the National Academy of Sciences USA, 94(7): 2796-2797. PDF

Nagi, A.D. and Regan, L.
An inverse correlation between loop length and stability in a four-helix-bundle protein.
Folding & Design, 2(1): 67-75. PDF

Munson, M., Anderson, K.S., and Regan, L.
Speeding up protein folding: mutations that increase the rate at which Rop folds
and unfolds by over four orders of magnitude.
Folding & Design, 2(1): 77-87. PDF

Dalal, S., Balasubramanian, S., and Regan, L.
Transmuting alpha helices and beta sheets.
Folding & Design, 2(5): R71-R79. PDF

Dalal, S., Balasubramanian, S., and Regan, L.
Protein alchemy: changing β-sheet into α-helix.
Nature Structural Biology, 4(7): 548-552. PDF


Smith, C.K., Bu, Z., Anderson, K.S., Sturtevant, J.M., Engelman, D.M., and Regan, L.
Surface point mutations that significantly alter the structure and stability of a protein's denatured state.
Protein Science, 5(10): 2009-2019. PDF

Predki, P.F., Agrawal, V., Brunger, A.T., and Regan, L.
Amino-acid substitutions in a surface turn modulate protein stability.
Nature Structural Biology, 3(1): 54-58. PDF

Munson, M., Balasubramanian, S., Fleming, K.G., Nagi, A.D., O'Brien, R., Sturtevant, J.M., and Regan, L.
What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties.
Protein Science, 5(8): 1584-1593. PDF


Smith, C.K., Munson, M., and Regan, L.
Studying α-helix and β-sheet formation in small proteins.
Techniques in Protein Chemistry, 6: 323-332.

Smith, C.K. and Regan, L.
Guidelines for protein design: the energetics of β sheet side chain interactions.
Science, 270(5238): 980-982. PDF

Regan, L.
Protein design: novel metal-binding sites.
Trends in Biochemical Sciences, 20(7): 280-285. PDF

Predki, P.F. and Regan, L.
Redesigning the topology of a four-helix-bundle protein: monomeric Rop.
Biochemistry, 34(31): 9834-9839. PDF

Predki, P.F., Nayak, L.M., Gottlieb, M.B., and Regan, L.
Dissecting RNA-protein interactions: RNA-RNA recognition by Rop.
Cell, 80(1): 41-50. PDF

Klemba, M. and Regan, L.
Characterization of metal binding by a designed protein:
single ligand substitutions at a tetrahedral Cys2His2 site.
Biochemistry, 34(31): 10094-10100. PDF

Klemba, M., Gardner, K.H., Marino, S., Clarke, N.D., and Regan, L.
Novel metal-binding proteins by design.
Nature Structural Biology, 2(5): 368-373. PDF


Smith, C.K., Withka, J.M., and Regan, L.
A thermodynamic scale for the beta-sheet forming tendencies of the amino acids.
Biochemistry, 33(18): 5510-5517. PDF

Regan, L., Rockwell, A., Wasserman, Z., and DeGrado, W.
Disulfide crosslinks to probe the structure and flexibility of a designed four-helix bundle protein.
Protein Science, 3(12): 2419-2427. PDF

Regan, L.
Protein structure. Born to be beta.
Current Biology, 4(7): 656-658. PDF

Munson, M., Predki, P.F., and Regan, L.
ColE1-compatible vectors for high-level expression of cloned DNAs from the T7 promoter.
Gene, 144(1): 59-62. PDF

Munson, M., O'Brien, R., Sturtevant, J.M., and Regan, L.
Redesigning the hydrophobic core of a four-helix-bundle protein.
Protein Science, 3(11): 2015-2022. PDF


Regan, L.
What determines where alpha-helices begin and end?
Proceedings of the National Academy of Sciences USA 90(23): 10907-10908. PDF

Regan, L.
The design of metal-binding sites in proteins.
Annual Review of Biophysics and Biomolecular Structure, 22: 257-287. PDF


Marqusee, S. and Regan, L.
Deconstructing protein structure.
Current Biology, 1(4): 207-208. PDF

Regan, L.
Protein design.
Current Opinion in Biotechnology, 2(4): 544-550. PubMed


Regan, L. and Clarke, N.
A tetrahedral Zn(II)-binding site introduced into a designed protein.
Biochemistry29(49): 10878-10883. PDF

Regan, L., Ho, S.P., Wasserman, Z., and Degrado, W.F.
Helical proteins: de novo design.
Protein Folding: Deciphering the Second Half of the Genetic Code.
ed. Gierasch, L.M. and King, J. Washington, D.C.: AAAS.


Regan, L. and DeGrado, W.F.
Characterization of a helical protein designed from first principles.
Science, 241(4868): 976-978. PDF

Regan, L., Buxbaum, L., Hill, K., and Schimmel, P.
Rationale for engineering an enzyme by introducing a mutation that compensates for a deletion.
Journal of Biological Chemistry, 263(35): 18598-18600. PDF

Frederick, C.A., Wang, A.H., Rich, A., Regan, L., and Schimmel, P.
Crystallization of a small fragment of an aminoacyl tRNA synthetase.
Journal of Molecular Biology, 203(2): 521-522. PDF


Regan, L. and Schimmel, P.
Selection of aminoacyl tRNA synthetases with enhanced catalytic activity.
UCLA Symposia on Molecular & Cellular Biology, 69: 293.

Regan, L., Bowie, J., and Schimmel, P.
Polypeptide sequences essential for RNA recognition by an enzyme.
Science, 235(4796): 1651-1653. PDF

DeGrado, W.F., Regan, L., and Ho, S.P.
The design of a four-helix bundle protein.
Cold Spring Harbor Symposia on Quantitative Biology, 52: 521-526. PubMed

DeGrado, W.F., Ho, S., Wasserman, Z., and Regan, L.
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Jasin, M., Regan, L., and Schimmel, P.
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