current research


1two 2rmm 4JGF


323. Qin J, Vinogradova O, Gronenborn AM.  Protein-protein interactions probed by NMR spectroscopy. Methods Enzymol 339: 377-389 (2001).

324. Gronenborn AM. Exploiting magnetic field induced alignment: Residual dipolar couplings for NMR structure determination. NATO ASI Series; Dynamics, Structure and Function of Biological Macromolecules 315: 107-116 (2001).

325. Barrientos LG, Campos-Olivas R, Louis JM, Fiser A, Sali A, Gronenborn AM. 1H, 13C, 15N resonance assignments and fold verification of a circular permuted variant of the potent HIV-inactivating protein cyanovirin-N. J Biolmol NMR 19: 289-290 (2001).

326. Barrientos LG, Louis JM, Gronenborn AM.  Characterization of the cholisteric phase of filamentous bacteriophage fd for molecular alignment. J Magn Reson 149: 154-158 (2001).

327. Campos-Olivas R, Hörr I, Bormann C, Jung G, Gronenborn AM.  Solution structure, backbone dynamics and chitin binding of the anti-fungal protein from Streptomyces Tendae TÜ901. J Mol Biol 308: 765-782 (2001).

328. Louis J M, Georgescu R, Tasayco M-L, Tcherkasskaya O, Gronenborn AM.  Probing the structure and stability of a hybrid protein: The human – E.coli thioredoxin chimera. Biochemistry 40: 11184-11192 (2001).

329. Dangi B, Pelupessey P, Martin RG, Rosner JL, Louis JM, Gronenborn AM. Structure and dynamics of MarA-DNA complexes: An NMR investigation. J Mol Biol 314: 113-127 (2001).

330. Ishima R, Ghirlando R, Tozser J, Gronenborn AM, Torchia DA, Louis JM.  Folded monomers of HIV-1 protease.  J Biol Chem 276 (52): 49110-49116 (2001).

331. Tcherkasskaya O, Klushin L, Gronenborn AM.  Effective lattice behavior of fluorescence energy transfer at lamellar macromolecular interfaces.  Biophysical J 82: 988-995 (2002).

332. Tcherkasskaya O, Gronenborn AM, Klushin L.  Excluded volume effect within the continuous model for the fluorescence energy transfer.  Biophys J 83: 2826-2834 (2002).

333. Barrientos LG, Louis JM, Hung J, Smith TH, O’Keefe BR, Gardella RS, Mori T, Boyd MR, Gronenborn AM.  Design and initial characterization of a circular permuted variant of the potent HIV-inactivating protein cyanovirin-N.  Proteins 46: 149-152 (2002).

334. Frank MK, Dyda F, Dobrodumov A, Gronenborn AM.  Core mutations switch monomeric protein GB1 into an intertwined tetramer.  Nat Struct Biol 9(11): 877-885 (2002).

335. Rosner JL, Dangi B, Gronenborn AM, Martin RG.  Post-translational activation of the transcriptional activator Rob by dipyridyl in Escherichia coli. J Bact 184: 1407-1416 (2002).

336. Barrientos LG, Louis JM, Botos I, Mori T, Han Z, O’Keefe BR, Boyd MR, Wlodawer A, Gronenborn AM.   The domain-swapped dimer of Cyanovirin-N is in a metastable folded state: Reconciliation of X-ray and NMR structures. Structure 10: 673-686 (2002).

337. Ding K, Gronenborn AM.  Novel 2D triple-resonance NMR experiments for sequential resonance assignments of proteins.  J Magn Reson 156: 262-268 (2002).

338. Campos-Olivas R, Aziz R, Helms GR, Evans JNS, Gronenborn AM.  Placement of 19F into the center of GB1: Effects on structure and stability. FEBS Lett 517: 55-60 (2002).

339. Barrientos LG, Gawrisch K, Cheng N, Stevens AC, Gronenborn AM.  Structural characterization of the dilute aqueous surfactant solution of cetylpyridinuium bromide/hexanol/sodium bromide.  Langmuir 18: 3773-3779 (2002).

340. Mori T, Barrientos LG, Han Z, Gronenborn AM, Turpin JA, Boyd MR.  Functional homologs of Cyanovirin-N amenable to mass production in prokaryotic and eukaryotic hosts.  Protein Expr Purif 26: 42-49 (2002).

341. Dangi B, Dobrodumov AV, Louis JM, Gronenborn AM.  Solution structure and dynamics of the human-E.coli thioredoxin chimera: Insights into thermodynamic stability.  Biochemistry 41: 9376-9388 (2002).

342. Campos-Olivas R, Louis JM, Clérot D, Gronenborn B, Gronenborn AM.  1H, 13C, and 15N assignment of the N-terminal, catalytic domain of the replication initiation protein from the geminivirus TYLCV.  J Biomol NMR 24: 73-74 (2002).

343. Campos-Olivas R, Louis JM, Clérot D, Gronenborn B, Gronenborn AM.  The structure of a replication initiator unites diverse aspects of nucleic acid metabolism. Proc Natl Acad Sci 99: 10319-10315 (2002).

344. Ermolenko DN, Thomas ST, Aurora R, Gronenborn AM, Makhatadze GL.  Hydrophobic interactions at the Ccap position of the C-capping motif of alpha-helices. J Mol Biol 322: 123-136 (2002).

345. Gronenborn AM.  The importance of being ordered- Improving NMR structures using residual dipolar couplings.  Comptes Rendus 325: 957-966 (2002).

346. Shenoy SR, Barrientos LG, Ratner DM, O’Keefe BR, Seeberger PH, Gronenborn AM, Boyd MR.  Multisite and multivalent binding between Cyanovirin-N and branched oligomannosides: Calorimetric and NMR characterization. Chem Biol 9: 1109-1118 (2002).

347. Ding K, Gronenborn AM.  Sensitivity-enhanced E.COSY-type HSQC experiments for accurate measurement of one-bond 15N-1HN and 15N-13C’ and two-bond 13C’-1HN residual dipolar couplings in proteins.  J Magn Reson 158: 173-177 (2002).

348. Barrientos LG,  Gronenborn AM. The domain-swapped dimer of cyanovirin-N contains two sets of oligosaccharide binding sites in solution.  Biochem Biophys Res Comm 298: 598-602 (2002).

349. Barrientos LG, O’Keefe BR, Bray M, Sanchez A, .Gronenborn AM, Boyd MR.  Cyanovirin-N binds to the viral surface glycoprotein GP1,2 and inhibits infectivity by Ebola virus. Antiviral Res 58: 47-56 (2003).

350. Barrientos LG, Louis JM, Ratner DM, Seeberger PH, Gronenborn AM.  Solution structure of a circular permuted variant of the potent HIV-inactivating protein cyanovirin-N: Structural basis for protein stability and oligosaccharide interaction. J Mol Biol 325:  211-233 (2003).

351. Mesleh MF, Valentine KG, Opella SJ, Louis JM, Gronenborn AM.  Myristoylation as a general method for immobilization and alignment of soluble proteins for solid-state NMR structural studies.  J Biomol NMR 25: 55-61 (2003).

352. Louis JM, Ishima R, Nesheiwat I, Pannell LK, Lynch SM, Torchia DA, Gronenborn AM. Revisiting monomeric HIV-1 protease – Characterization and redesign for improved properties.  J Biol Chem 278: 6085-6092 (2003).

353. Gronenborn AM.  Rapid screening of E. coli extracts by heteronuclear NMR.  Curr Protoc Protein Sci, unit 7.11 (2003).

354. Dobrodumov A, Gronenborn AM.  Filtering and selection of structural models: Combining docking and NMR.  Proteins 53: 18-32 (2003).

355. Ding K, Gronenborn AM.  Sensitivity-enhanced 2D IPAP, TROSY-anti-TROSY and E.COSY experiments: Alternatives for measuring dipolar 15N-1HN couplings.  J Magn Reson 163: 208-214 (2003).

356. Ding K, Gronenborn AM.  Simultaneous and accurate determination of one-bond 15N-13C’ and two-bond 1HN-13C’ dipolar couplings.  J Am Chem Soc 125: 11504-11505 (2003).

357. Byeon I-JL, Louis JM, Gronenborn AM.  A protein contortionist: Core mutations of GB1 that induce dimerization and domain-swapping.  J Mol Biol 333: 141-152 (2003).

358. Katoh E, Louis JM, Yamazaki T, Gronenborn AM, Torchia DA, Ishima I.  A solution NMR study of the binding kinetics and the internal dynamics of HIV-1 protease-substrate complex.  Protein Sci 12: 1376-1385 (2003).

359. Ishima R, Torchia DA, Lynch SM, Gronenborn AM, Louis JM. Solution  structure of the mature HIV-1 protease monomer: Insight into the tertiary fold and stability of a precursor. J Biol Chem 278: 43311-43319 (2003).

360. McKinney J, Knappskog PM, Pereira J, Ekern T, Toska K, Kuitert BB, Levine D, Gronenborn AM, Martinez A, Haavik J.  Expression and purification of  human Tryptophan Hydroxylase form Escherichia coli and Pichia pasoris. Protein Expr Purif 33: 185-194 (2004).

361. Ding K, Louis JM, Gronenborn AM.  Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR.  J Mol Biol 335:  1299-1307 (2004).

362. Mohanty S, Zubkov S, Gronenborn AM.  The solution NMR structure of Antheraea polyphemus PBP provides new insight on pheromone recognition by pheromone binding proteins.  J Mol Biol 337: 443-451 (2004).

363. Ding K, Gronenborn AM.  Sensitivity-enhanced IPAP experiments for measuring one-bond 13C’-13C and 13C-1H residual dipolar couplings in proteins.  J Magn Reson 167: 253-258 (2004).

364. Byeon I-JL, Louis JM, Gronenborn AM.  A captured folding intermediate involved in dimerization and domain-swapping of GB1.  J Mol Biol 340: 615-625 (2004).

365. Ding K, Gronenborn AM.  Protein backbone 1HN-13C and 15N- 13C residual dipolar and J couplings: New constraints for NMR structure determination.  J Am Chem Soc 126: 6232-6233 (2004).

366. Dangi B, Gronenborn AM, Rosner JL, Martin RG.  Versatility of the carboxy-terminal domain of the  subunit of RNA polymerase in transcriptional activation: Use of the DNA contact site as a protein contact site for MarA. Mol Microbiol 54: 45-59 (2004).

367. Barrientos LG, Lasala F, Delgado R, Sanchez A, Gronenborn AM.  Flipping the switch from monomeric to dimeric CV-N has little effect on antiviral activity.  Structure 12: 1799-1807 (2004).

368. Sanderström C, Berteau O, Gemma E, Oscarson S, Kenne L, Gronenborn AM.  Atomic mapping of the interactions between the antiviral agent cyanovirin-N and oligomannosides by saturation-transfer difference NMR. Biochemistry 43: 13926-13931 (2004).

369. Barrientos LG, Gronenborn AM.  The highly specific carbohydrate-binding protein cyanovirin-N: Structure, Anti-HIV/Ebola activity and possibilities for therapy. Mini Rev Med Chem 5: 21-31 (2005).

370. Louis JM, Byeon, I-J L, Baxa U, Gronenborn AM.  The GB1 amyloid fibril – Recruitment of the peripheral - strands of the domain swapped dimer into the polymeric interface. J Mol Biol 348: 687-698 (2005).

371. Mangold SL, Morgan JR, Strohmeyer GC, Gronenborn AM, Cloninger MJ.  Cyanovirin-N binding to Man 1-2Man functionalized dendrimers.  Org Biomol Chem 3: 2354 – 2358 (2005).

372. Byeon I-JL, Li H, Song H, Gronenborn AM, Tsai M-D. Sequential phosphorylation and multisite interactions characterize specific target recognition by the FHA domain of Ki67.  Nat Struct Mol Biol 12: 987-993 (2005).

373. Zubkov S, Gronenborn AM,  Byeon I-JL, Mohanty S. Structural consequences of the pH-induced conformational switch in A. polyphemus pheromone binding protein: mechanisms of ligand release.  J Mol Biol 354: 1081-1090 (2005).