{"id":4478,"date":"2025-07-22T21:07:55","date_gmt":"2025-07-22T21:07:55","guid":{"rendered":"https:\/\/montelionelab.chem.rpi.edu\/?page_id=4478"},"modified":"2025-07-22T21:07:55","modified_gmt":"2025-07-22T21:07:55","slug":"publications-2000-prior","status":"publish","type":"page","link":"https:\/\/montelionelab.chem.rpi.edu\/index.php\/publications-2000-prior\/","title":{"rendered":"Publications 2000 & Prior"},"content":{"rendered":"\n
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2000<\/h6>\n\n\n\n

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1. Xiong Y; Juminaga D; Swapna GVT; Wedemayer WJ; Scheraga HA; Montelione GT.  Protein Science<\/strong>. 2000, 9: 421 – 426. Solution NMR evidence for a cis Tyr-Ala peptide group in the structure of [Pro93Ala] bovine pancreatic ribonuclease A.<\/a>  PMC2144552<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

2. McDermott A; Polenova T; Bockmann A; Zilm KW; Paulson EK; Martin RW; Montelione GT. J. Biomol. NMR. <\/strong>2000, 16: 209 \u2013 219. Partial NMR resonance assignments of uniformly (13<\/sup>C,15<\/sup>N)-labeled BPTI in the solid state.<\/a> Pubmed<\/a>.<\/p>\n\n\n\n

3. Montelione GT; Anderson S. The Investigational Drugs Database (IDdb)<\/strong>. March 15, 2000.  Quantitative challenges in the post-genomic sequence era.<\/p>\n\n\n\n

4. Andrec M; Inman KG; Weber DJ; Levy RM; Montelione GT. J. Magn. Reson. <\/strong>2000, 146: 66 – 80. A Bayesian statistical method for the detection and qualification of rotational diffusion anistropy from NMR relaxational data.<\/a> Pubmed<\/a>. <\/p>\n\n\n\n

5. Andrec M; Montelione GT; Levy, R.  J. Biomol. NMR<\/strong>. 2000, 18: 83 – 100.  Lipari-Szabo mapping: A graphical approach to Lipari-Szabo analysis of NMR relaxation data using reduced spectral density mapping.<\/a> Pubmed<\/a>.<\/p>\n\n\n\n

6. Montelione GT; Zheng D; Huang YJ; Gunsalus KC; Szyperski; T.  Nature Struct. Biol.<\/strong> 2000, 7: 982 – 985. Protein NMR spectroscopy in structural genomics<\/a>. Pubmed<\/a>.<\/p>\n<\/div>\n<\/div>\n\n\n\n

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1999<\/h6>\n<\/div>\n\n\n\n
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1. Montelione GT; Anderson; S. Nature Struct. Biol. <\/strong>1999, 6: 11 – 12. Structural genomics: Keystone for a human proteome project<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

2. Wang W; Riedel K; Lynch P; Chien CY; Montelione GT; Krug RM. RNA. <\/strong>1999, 5: 195 – 205. RNA-binding by the novel helical domain of the Influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids<\/a>.  PMC1369752<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

3. Swapna GVT; Montelione GT. J. Magn. Reson.<\/strong> 1999, 137: 437 \u2013 442. Sensitivity-enhanced Sim-CT HMQC PFG-HBHA(CO)NH and PFG-CBCA(CO)NH triple-resonance experiments.<\/a> Pubmed<\/a>.<\/p>\n\n\n\n

4. Andrec M; Montelione GT; Levy RM. J. Magn. Reson.<\/strong> 1999, 139: 408 – 421. Estimation of dynamic parameters from NMR relaxation data using the Lipari-Szabo Model-free approach and Bayesian statistical methods.<\/a> Pubmed<\/a>.<\/p>\n\n\n\n

5. Moseley HNB; Montelione, GT.  Curr. Opin. Struct. Biol.<\/strong> 1999, 9: 635 – 642.  Automated analysis of NMR assignments and structures for proteins.<\/a> Pubmed<\/a>.<\/p>\n\n\n\n

6. Tejero R; Monleon D; Celda B; Montelione GT. J. Biomol. NMR<\/strong>. 1999, 15: 251 – 264. HYPER: A hierarchical algorithm for automatic determination of protein dihedral-angle constraints and stereospecific C \u03b2<\/sup>H2<\/sub> resonance assignments from NMR data.<\/a> <\/p>\n\n\n\n

7. Laity JH; Montelione GT; Scheraga HA. Biochemistry<\/strong>. 1999, 38: 16432 – 16442.  Comparison of local and global stability of an analogue of a disulfide-folding intermediate with those of the wild-type protein in bovine pancreatic ribonuclease A: Identification of specific regions of stable structure along the oxidative folding pathway.<\/a>  suppl. material<\/a>. Pubmed<\/a>. <\/p>\n\n\n\n

8. Montelione GT; Rios CB; Swapna GVT; Zimmerman DE. 1999, Biological Magnetic Resonance, <\/strong>v 17: Structural Computation and Dynamics in Protein NMR,<\/strong> pp. 81 – 130. NMR pulse sequences and computational approaches for automated analysis of sequence- specific backbone resonance assignments in proteins.<\/a> ‘<\/p>\n<\/div>\n<\/div>\n\n\n\n

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1998<\/h6>\n<\/div>\n\n\n\n
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1. Sahasrabudhe PV; Tejero R; Kitao S; Furuichi Y; Montelione GT. PROTEINS: Struct. Funct. Genetics<\/strong>. 1998, 33: 558 – 566. Homology modeling of an RNP domain from a human RNA-binding protein: Homology-constrained energy optimization provides a criterion for distinguishing potential sequence alignments.<\/a> Pubmed<\/a>.<\/p>\n\n\n\n

2. Feng W; Tejero R; Zimmerman DE; Inouye M; Montelione GT. Biochemistry<\/strong>. 1998, 37: 10881 – 10896. Solution NMR structure and backbone dynamics of the major cold shock protein (CspA) from Escherichia coli<\/em> Evidence for conformational dynamics in the ssRNA- binding site.<\/a>  suppl. material<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

3. Montelione GT; Farid RS; Hitchcock-DeGregori SE. Biochemistry<\/strong>. 1998, 37: 7834 – 7843. The structure of the N-terminus of striated muscle \u03b1-tropomyosin in a chimeric peptide: Solution NMR structure and circular dichroism studies.<\/a>  suppl. material<\/a>.<\/p>\n\n\n\n

4. Mullenbach GT; Chiu CY; Gyenes A; Blaney J; Rosenberg S; Marlowe CK; Brown S; Stratton-Thomas J; Montelione GT; George- Nascimento C; Stauber G.  Protein Engineering<\/strong>. 1998, 11: 473 \u2013 480. Modification of a receptor-binding surface of epidermal growth factor (EGF): Analogs with enhanced receptor affinity at low pH or at neutrality<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

5. Jin, D; Andrec M; Montelione GT; Levy RM. J. Biomol. NMR. <\/strong>1998, 12: 471 – 492. Propagation of experimental uncertainties using the Lipari-Szabo model-free analysis of protein dynamics.<\/a> Pubmed<\/a>. <\/p>\n\n\n\n

6. Kulikowski CA; Zimmerman D; Montelione GT; Anderson S. Stud. Health Technol. Inform. <\/strong>1998, 52 Pt. 1: 365-366.  Structural- functional bioinformatics: Knowledge-based NMR interpretation.<\/a> <\/p>\n<\/div>\n<\/div>\n\n\n\n

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1997<\/h6>\n<\/div>\n\n\n\n
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1. Swapna GVT; R\u00edos CB; Shang Z; Montelione GT. J. Biomol. NMR. <\/strong>1997, 9: 105 – 111. Application of multiple-quantum line narrowing with simultaneous 1<\/sup>H and 13<\/sup>C constant-time scalar- coupling evolution in PFG-HACANH and PFG-HACA(CO)NH triple-resonance experiments<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

2. Li H; Tejero R; Monleon D; Bassolino-Klimas D; Abate-Shen C; Bruccoleri RE; Montelione GT.  Protein Science<\/strong>. 1997, 6: 956 – 970. Homology modeling using simulated annealing of restrained molecular dynamics and conformational search calculations with CONGEN: Application in predicting the three-dimensional structure of murine homeodomain Msx-1<\/a>.  PMC2143703<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

3. Zimmerman DE; Kulikowski CA; Huang Y; Feng W; Tashiro M; Shimotakahara S; Chien CY; Powers R; Montelione GT. J. Mol. Biol. <\/strong>1997, 269: 592 – 610. Automated analysis of protein NMR assignments using methods from artificial intelligence.<\/a> Pubmed<\/a>.<\/p>\n\n\n\n

4. Shimotakahara S; R\u00edos CB; Laity JH; Zimmerman DE; Scheraga HA; Montelione GT. Biochemistry<\/strong>. 1997, 36 : 6915 \u2013 6929.  NMR structural analysis of an analog of an intermediate formed in the rate-determining step of one pathway in the oxidative folding of bovine pancreatic ribonuclease A: Automated analysis of 1<\/sup>H, 13<\/sup>C, and 15<\/sup>N resonance assignments for wild-type and [C65S, C72S] mutant forms<\/a>.  suppl. material<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

5. Laity JH; Lester C; Shimotakahara S; Zimmerman DE; Montelione GT; Scheraga HA. Biochemistry. <\/strong>1997, 36: 12683 – 12699. Structural characterization of an analog of the major rate-determining disulfide folding intermediate of bovine pancreatic ribonuclease A<\/a>.  suppl. material<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

6. Shang Z; Swapna GVT; R\u00edos CB; Montelione GT. J. Am. Chem. Soc.<\/strong> 1997, 119: 9274 – 9278. Sensitivity enhancement of triple-resonance protein NMR spectra by proton evolution of multiple-quantum coherences using a simultaneous 1<\/sup>H and 13<\/sup>C constant-time evolution period<\/a>. <\/p>\n\n\n\n

7. Tashiro M; Tejero R; Zimmerman DE; Celda B; Nilsson B; Montelione GT. J. Mol. Biol.<\/strong> 1997, 272: 573 – 590. High resolution solution NMR structure of the Z domain of staphylococcal protein A<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

8. Chien CY; Tejero R; Huang Y; Zimmerman DE; Krug RM; Montelione GT.  Nature Struct. Biol.<\/strong> 1997, 4: 891 \u2013 895.  A novel RNA-binding motif in influenza A virus non-structural protein 1.<\/a> Pubmed<\/a>.<\/p>\n\n\n\n

9. Liu J; Lynch P; Chien CY; Montelione GT; Krug RM; Berman H. Nature Struct. Biol. <\/strong>1997, 4: 896 – 899. Crystal structure of the unique RNA- binding domain of the influenza virus NS1 protein<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

10. Jin D; Figueirido F; Montelione GT; Levy RM. J. Am. Chem. Soc.<\/strong> 1997, 119: 6923 – 6924. Impact of the precision in NMR relaxation measurements on the interpretation of protein dynamics<\/a>. <\/p>\n<\/div>\n<\/div>\n\n\n\n

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1996<\/h6>\n<\/div>\n\n\n\n
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1. Jendeberg L; Tashiro M; Tejero R; Lyons BA; Uhl\u00e9n M; Montelione GT; Nilsson B. Biochemistry <\/strong>1996, 35: 22 – 31. The mechanism of binding staphylococcal protein A to immunoglobulin G does not involve helix unwinding.<\/a> Pubmed<\/a>.<\/p>\n\n\n\n

2. Jansson M; Li YC; Jendeberg L; Anderson S; Montelione GT; Nilsson B. J. Biomol. NMR. <\/strong>1996, 7: 131 – 141. High- level production of uniformly 15<\/sup>N-and 13<\/sup>C-enriched fusion proteins in Escherichia coli.<\/em><\/a> Pubmed<\/a>.<\/p>\n\n\n\n

3. Bassolino-Klimas D; Tejero R; Krystek SR; Metzler WJ; Montelione GT; Bruccoleri RE.  Protein Science<\/strong>. 1996, 5: 593 – 603. Simulated annealing with restrained molecular dynamics using a flexible restraint potential: Theory and evaluation with simulated NMR constraints<\/a>.  PMC2143380<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

4. Tejero R; Bassolino-Klimas D; Bruccoleri RE; Montelione GT.  Protein Science<\/strong>. 1996, 5: 578 – 592. Simulated annealing with restrained molecular dynamics using CONGEN: Energy refinement of the NMR solution structures of epidermal and type-\u03b1 transforming growth factors<\/a>.  PMC2143379<\/a>.<\/p>\n\n\n\n

5. Feng W; R\u00edos CB; Montelione G. T. J. Biomol. NMR. <\/strong>1996, 8: 98 – 104. Phase labeling of C-H and C-C spin-system topologies: Applications in PFG-HACANH and PFG-HACA(CO)NH triple-resonance experiments for determining backbone resonance assignments in proteins<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

6. R\u00edos CB; Feng W; Tashiro M; Shang Z; Montelione GT. J. Biomol. NMR<\/strong>. 1996, 8: 345 – 350. Phase labeling of C-H and C-C spin system topologies: Application in constant-time PFG-CBCA(CO)NH experiments for discriminating amino-acid spin-system types<\/a>. Pubmed<\/a>.<\/p>\n<\/div>\n<\/div>\n\n\n\n

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1995<\/h6>\n<\/div>\n\n\n\n
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1. Tashiro M; Montelione GT. Current Opin. In Struct. Biol. <\/strong>1995, 5: 471 – 481. Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

2. Zimmerman DE; Montelione GT. Current Opin. in Struct. Biol. <\/strong>1995, 5: 664 – 673. Automated analysis of nuclear magnetic resonance assignments for proteins<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

3. Celda B; Biamonti C; Arnau MJ; Tejero R; Montelione GT. J. Biomol. NMR. <\/strong>1995, 5: 161 – 172. Combined use of 13<\/sup>C chemical shift and 1<\/sup>H\u03b1<\/sup>–13<\/sup>C\u03b1<\/sup> heteronuclear NOE data in monitoring a protein NMR structure refinement<\/a>. Pubmed<\/a>. <\/p>\n\n\n\n

4. Li YC; Montelione GT. Biochemistry<\/strong>. 1995, 34: 2408 – 2423. Human type- \u03b1 transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by 15<\/sup>N relaxation measurements.<\/a> Pubmed<\/a>.<\/p>\n\n\n\n

5. Tashiro M; R\u00edos CB, Montelione GT. J. Biomol. NMR<\/strong>. 1995, 6: 211 – 216.  Classification of amino acid spin systems using PFG HCC(CO)NH-TOCSY with constant-time aliphatic carbon-13 frequency labeling<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

6. Fadel AR; Jin DQ; Montelione GT; Levy RM. J. Biomol. NMR<\/strong>. 1995, 6: 221 – 226. Crankshaft motions of the polypeptide backbone in molecular dynamics simulations of human type-\u03b1 transforming growth factor<\/a>. Pubmed<\/a>.<\/p>\n\n\n\n

7. Qian XY; Chien CY; Lu Y; Montelione GT; Krug RM. RNA<\/strong>. 1995, 1: 948 – 956. An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure<\/a>.  PMC1369343<\/a>.<\/p>\n<\/div>\n<\/div>\n\n\n\n

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1994<\/h6>\n<\/div>\n\n\n\n
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1. Campion SR; Biamonti C; Montelione GT; Niyogi SK. Protein Engineering<\/strong>. 1993, 6: 651 – 659. The role of asparagine-32 in forming the receptor-binding epitope of human epidermal growth factor. (featured on cover of August 1994 issue of Protein Engineering)<\/a>. <\/p>\n\n\n\n

2. Lyons BA; Tashiro M; Cedergren L, Nilsson B; Montelione GT. Biochemistry<\/strong>. 1993, 32: 7839 – 7845.  An improved strategy for determining resonance assignments for isotopically enriched proteins and its application on an engineered domain of staphylococcal Protein A<\/a>. <\/p>\n\n\n\n

3. Li YC; Montelione GT. J. Magn. Reson.<\/strong> 1993, B101: 315 – 319. Solvent saturation-transfer effects in pulsed-field-gradient heteronuclear single- quantum coherence (PFG-HSQC) spectra of polypeptides and proteins<\/a>. <\/p>\n\n\n\n

4. Zimmerman D; Kulikowski C; Montelione GT. Proc. Int. Conf. Intell. Syst. Mol. Biol.<\/strong> 1993, 1: 447 – 455. A constraint reasoning system for automating sequence-specific resonance assignments in multidimensional protein NMR spectra<\/a>. <\/p>\n\n\n\n

5. Zimmerman D; Kulikowski C; Wang L; Lyons B; Montelione GT. J. Biomol. NMR<\/strong>. 1994, 4: 241 – 256. Automated sequencing of amino acid spin systems in proteins using multidimensional HCC(CO)NH-TOCSY spectroscopy and constraint propagation methods from artificial intelligence<\/a>. <\/p>\n\n\n\n

6. Li YC; Montelione GT. J. Magn. Reson.<\/strong> 1994, 105: 45 – 51. Overcoming solvent saturation-transfer artifacts in protein NMR at neutral pH: Application of pulsed-field gradients in measurements of1<\/sup>H- 15<\/sup>N Overhauser effects<\/a>. <\/p>\n\n\n\n

7. Newkirk K; Feng W; Jiang W; Tejero R; Emerson SD; Inouye M; Montelione GT. Proc. Natl. Acad. Sci. U.S.A. <\/strong>1994, 91: 5114 – 5118. Solution NMR structure of the major cold-shock protein (CspA) from Escherichia coli<\/em> : Identification of a binding epitope for DNA.<\/a>  PMC43942<\/a>.<\/p>\n\n\n\n

8. Shang Z; Isaac VE; Li H; Patel L; Catron KM; Curran T; Montelione GT; Abate C. Proc. Natl. Acad. Sci. U.S.A.<\/strong> 1994, 91: 8373 – 8377. Design of a “minimA1” homeodomain: the N- terminal arm modulates DNA binding affinity and stabilizes homeodomain structure.<\/a>  PMC44608<\/a>.<\/p>\n\n\n\n

9. Biamonti C; R\u00edos CB; Lyons BA; Montelione GT. Advances in Biophysical Chemistry<\/strong>. 1994, 4: 51 – 120. Multidimensional NMR experiments and analysis techniques for determining homo- and heteronuclear scalar coupling constants in proteins and nucleic acids.<\/a> <\/p>\n<\/div>\n<\/div>\n\n\n\n

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1993<\/h6>\n<\/div>\n\n\n\n
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1. Lyons BA; Montelione GT. J. Magn. Reson. <\/strong>1993, B101: 206 \u2013 209. An HCCNH triple-resonance experiment using carbon-13 isotropic mixing for correlating backbone amide and side-chain aliphatic resonances in isotopically enriched proteins<\/a>.<\/p>\n\n\n\n

2. Celda B; Montelione GT. J. Magn. Reson. <\/strong>1993, B101: 189 – 193. Total correlation spectroscopy (TOCSY) of proteins using coaddition of spectra recorded with several mixing times<\/a>. <\/p>\n\n\n\n

3. Moy FJ; Li YC; Rauenbuehler P; Winkler ME; Scheraga HA; Montelione GT. Biochemistry<\/strong>. 1993, 32: 7334 – 7353. Solution structure of human type-\u03b1 transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints<\/a>.  suppl. material<\/a>.<\/p>\n\n\n\n

4. Campion SR; Biamonti C; Montelione GT; Niyogi SK. Protein Engineering<\/strong>. 1993, 6: 651 – 659. The role of asparagine-32 in forming the receptor-binding epitope of human epidermal growth factor. (featured on cover of August 1994 issue of Protein Engineering)<\/a>. <\/p>\n\n\n\n

5. Lyons BA; Tashiro M; Cedergren L; Nilsson B; Montelione GT. Biochemistry<\/strong>. 1993, 32: 7839 – 7845.  An improved strategy for determining resonance assignments for isotopically enriched proteins and its application on an engineered domain of staphylococcal Protein A<\/a>. <\/p>\n\n\n\n

6. Li YC; Montelione GT. J. Magn. Reson.<\/strong> 1993, B101: 315 – 319. Solvent saturation-transfer effects in pulsed-field-gradient heteronuclear single- quantum coherence (PFG-HSQC) spectra of polypeptides and proteins<\/a>. <\/p>\n\n\n\n

7. Zimmerman D; Kulikowski C; Montelione GT. Proc. Int. Conf. Intell. Syst. Mol. Biol.<\/strong> 1993, 1: 447 – 455. A constraint reasoning system for automating sequence-specific resonance assignments in multidimensional protein NMR spectra<\/a>. <\/p>\n<\/div>\n<\/div>\n\n\n\n

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1992<\/h6>\n<\/div>\n\n\n\n
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1. Montelione GT; W\u00fcthrich K; Burgess AW; Nice EC; Wagner G; Gibson KD; Scheraga HA. Biochemistry<\/strong>. 1992, 31: 236 – 249. Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints.<\/a> <\/p>\n\n\n\n

2. Emerson SD; Montelione GT. J. Amer. Chem. Soc.<\/strong> 1992, 114: 354 – 356. Accurate measurements of proton scalar coupling constants using carbon-13 isotropic mixing spectroscopy.<\/a> <\/p>\n\n\n\n

3. Montelione GT; Emerson SD; Lyons BA. Biopolymers<\/strong>. 1992, 32: 327 – 334. A general approach for determining scalar coupling constants in polypeptides and proteins<\/a>. <\/p>\n\n\n\n

4. Moy FJ; Scheraga HA; Patt SL; Montelione GT. J. Magn. Reson.<\/strong> 1992, 98: 451 – 457. Application of frequency-shifted shaped pulses for overcoming solvent-saturation transfer and pre-irradiation associated spin-diffusion effects in aqueous solutions of polypeptides and proteins.<\/a> <\/p>\n\n\n\n

5. Emerson SD; Montelione GT. J. Magn. Reson.<\/strong> 1992, 99: 413 \u2013 420. 2D and 3D HCCH TOCSY experiments for determining 3<\/sup>J(H\u03b1<\/sup>-H\u03b2<\/sup>) coupling constants of amino acid residues.<\/a> <\/p>\n\n\n\n

6. Montelione GT; Lyons BA; Emerson SD; Tashiro M. J. Amer. Chem. Soc.<\/strong> 1992, 114: 10974 – 10975. An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically enriched proteins<\/a>. suppl. material<\/a>.<\/p>\n<\/div>\n<\/div>\n\n\n\n

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1990<\/h6>\n<\/div>\n\n\n\n
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1. Wagner G; Nirmala NR; Montelione GT; Hyberts S. Frontiers of NMR in Molecular Biology<\/strong>. 129 – 143. 1990. A.R. Liss, Inc., New York, NY. Static and dynamic aspects of protein structure.<\/a> <\/p>\n\n\n\n

2. Montelione, G.T.; Wagner, G. J. Magn. Reson.<\/strong> 1990, 87: 183 – 188. Conformation-independent sequential NMR connections in isotope-enriched polypeptides by 1<\/sup>H-13<\/sup>C- 15<\/sup>N triple-resonance experiments.<\/a> <\/p>\n\n\n\n

3. Engler, D.A.; Montelione, G.T.; Niyogi, S.K. FEBS Lett.<\/strong> 1990, 271: 47 – 50. Human epidermal growth factor: Distinct roles of Tyr-37 and Arg-41 in receptor binding as determined by site-directed mutagenesis and nuclear magnetic resonance spectroscopy.<\/a> <\/p>\n<\/div>\n<\/div>\n\n\n\n

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1989<\/h6>\n<\/div>\n\n\n\n
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1. Montelione, G.T.; Winkler, M.E.; Burton, L.E.;Rinderknecht, E.; Sporn, M.B.; Wagner, G. Proc. Natl. Acad. Sci. U.S.A.<\/strong> 1989, 86: 1519 – 1523. Sequence-specific 1<\/sup>H-NMR assignments and identification of two small anti-parallel \u03b2-sheets in the solution structure of recombinant human transforming growth factor-\u03b1<\/a>.  PMC286729<\/a><\/p>\n\n\n\n

2. Montelione, G.T.; Wagner, G. J. Amer. Chem. Soc.<\/strong> 1989, 111: 3096 \u2013 3098. 2D chemical exchange NMR spectroscopy by proton-detected heteronuclear correlation.<\/a> <\/p>\n\n\n\n

3. Montelione, G.T.; Winkler, M.; Rauenbuehler, P.; Wagner,G. J. Magn. Reson.<\/strong> 1989, 82: 198 – 204. Accurate measurements of long-range heteronuclear coupling constants from homonuclear 2D NMR spectra of isotope- enriched proteins.<\/a> <\/p>\n\n\n\n

4. Montelione, G.T.; Wagner, G. J. Amer. Chem. Soc.<\/strong> 1989, 111: 5474 \u2013 5475. Accurate measurements of homonuclear HN<\/sup>-H\u03b1<\/sup> coupling constants in polypeptides using heteronuclear 2D NMR experiments<\/a>. (pdf)<\/p>\n\n\n\n

5. Moy, F.J.; Scheraga, H.A.; Liu, J.-F.; Wu, R.; Montelione, G.T. Proc. Natl. Acad. Sci. U.S.A.<\/strong> 1989, 86: 9836 – 9840. Conformational characterization of a single-site mutant of murine epidermal growth factor (EGF) by 1<\/sup>H-NMR provides evidence that leucine-47 is involved in interactions with the EGF receptor.<\/a>  PMC298597<\/a><\/p>\n\n\n\n

6. Montelione, G.T.; Scheraga, H.A.  Accts. Chem. Research<\/strong> 1989, 22: 70 – 76. Formation of local structures in protein folding.<\/a> <\/p>\n<\/div>\n<\/div>\n\n\n\n

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1988<\/h6>\n<\/div>\n\n\n\n
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1. Montelione, G.T.; W\u00fcthrich, K.; Scheraga, H.A. Biochemistry<\/strong> 1988, 27: 2235 – 2243. Sequence-specific 1<\/sup>H-NMR assignments and identification of slowly exchanging amide protons in murine epidermal growth factor<\/a>. suppl. material<\/a> <\/p>\n\n\n\n

2. Ray, P.; Moy, F.; Montelione, G.T.; Liu, J.-F.; Narang, S.A.; Scheraga, H.A.; Wu, R. Biochemistry<\/strong> 1988, 27: 7289 – 7295. Structure- function studies of murine epidermal growth factor: Expression and site- directed mutagenesis of the epidermal growth factor gene.<\/a> <\/p>\n<\/div>\n<\/div>\n\n\n\n

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1987<\/h6>\n<\/div>\n\n\n\n
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1. Talluri S; Montelione GT; Van Duyne G; Piela L; Clardy J; Scheraga HA. J. Amer. Chem. Soc.<\/strong> 1987, 109: 4473 – 4477. Conformational properties of 2,4-methanoproline (2,carboxy-2,4-methanopyrrolidine) in peptides: Evidence for 2,4-methanopyrrolidine asymmetry based on solid state X-ray crystallography, 1<\/sup>H-NMR in aqueous solution, and CNDO\/2 conformational energy calculations<\/a>.  suppl. material<\/a>.<\/p>\n\n\n\n

2. Haas E; Montelione GT; McWherter CA; Scheraga HA. Biochemistry<\/strong>. 1987, 26: 1672 – 1682. Local structure in a tryptic fragment of performic acid oxidized ribonuclease A corresponding to a proposed polypeptide chain-folding initiation site detected by tyrosine fluorescence lifetime and proton magnetic resonance measurements<\/a>. <\/p>\n\n\n\n

3. Montelione GT; W\u00fcthrich K; Nice EC; Burgess AW; Scheraga HA. Proc. Natl. Acad. Sci. U.S.A.<\/strong> 1987, 84: 5226 – 5230. Solution structure of murine epidermal growth factor: Determination of the polypeptide backbone chain-fold by nuclear magnetic resonance and distance geometry.<\/a>  PMC298827<\/a>.<\/p>\n<\/div>\n<\/div>\n\n\n\n

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1986<\/h6>\n<\/div>\n\n\n\n
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1. Stimson ER; Meinwald YC; Montelione GT; Scheraga HA. Intl. J. Peptide Protein Res.<\/strong> 1986, 27: 569 – 582. Conformational properties of trans<\/em> Ac- Asn-Pro-Tyr-NHMe and trans<\/em> Ac-Tyr-Pro-Asn-NHMe in dimethylsulfoxide and in water determined by multinuclear NMR spectroscopy.<\/a> <\/p>\n\n\n\n

2. Montelione GT; Hughes P; Clardy J; Scheraga HA. J. Amer. Chem. Soc.<\/strong> 1986, 108: 6765 – 6773. Conformational properties of 2,4-methanoproline (2-carboxy-2,4-methanopyrrolidine) in peptides: Determination of preferred peptide bond conformations in aqueous solution by proton Overhauser measurements<\/a>. <\/p>\n\n\n\n

3. Montelione GT; W\u00fcthrich K; Nice EC; Burgess AW; Scheraga HA. Proc. Natl. Acad. Sci. U.S.A.<\/strong> 1986, 83: 8594 – 8598. Identification of two anti-parallel beta-sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance.<\/a>  PMC386977<\/a>.<\/p>\n<\/div>\n<\/div>\n\n\n\n

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1984<\/h6>\n<\/div>\n\n\n\n
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1. Montelione GT; Arnold E; Meinwald YC; Stimson ER; Denton JB; Huang SG; Clardy J; Scheraga HA. J. Amer. Chem. Soc.<\/strong> 1984, 106: 7946 – 7958. Chain-folding initiation structures in ribonuclease A: Conformational analysis of trans<\/em> Ac-Asn-Pro-Tyr-NHMe and trans<\/em> Ac-Tyr-Pro-Asn-NHMe in water and in the solid state<\/a>.  suppl. material<\/a>  addition\/correction<\/a>. <\/p>\n\n\n\n

2. Oka M; Montelione GT; Scheraga HA. J. Amer. Chem. Soc.<\/strong> 1984, 106: 7959 – 7969. Chain-folding initiation structures in ribonuclease A: Conformational free energy calculations on Ac-Asn-Pro-Tyr- NHMe, Ac-Tyr-Pro-Asn-NHMe, and related peptides<\/a>.  suppl. material<\/a>. <\/p>\n\n\n\n

3. Swadesh JK; Montelione GT; Thannhauser TW; Scheraga HA. Proc. Natl. Acad. Sci. U.S.A.<\/strong> 1984, 81: 4606 – 4610. Local structure involving histidine-12 in reduced S-sulfonated ribonuclease A detected by proton NMR spectroscopy under folding conditions<\/a>.  PMC345642<\/a>.<\/p>\n<\/div>\n<\/div>\n\n\n\n

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1982<\/h6>\n<\/div>\n\n\n\n
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1. Stimson ER; Montelione GT; Meinwald YC; Rudolph RKE; Scheraga HA. Biochemistry<\/strong>. 1982, 21: 5252 – 5262. Equilibrium ratios of cis<\/em>– and trans<\/em>-proline conformers in fragments of ribonuclease A from nuclear magnetic resonance spectra of adjacent tyrosine ring resonances<\/a>.  suppl. material<\/a>. <\/p>\n<\/div>\n<\/div>\n\n\n\n

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1981<\/h6>\n<\/div>\n\n\n\n
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1. Montelione, G.T.; Callahan, S.; Podleski, T.R. Biochim. Biophys. Acta 1981 <\/strong>, 670: 110 – 123. Physical and chemical characterization of the major lactose-blockable lectin activity from fetal calf skeletal muscle<\/a>. <\/p>\n<\/div>\n<\/div>\n\n\n\n

<\/p>\n","protected":false},"excerpt":{"rendered":"

2000 1. Xiong Y; Juminaga D; Swapna GVT; Wedemayer WJ; Scheraga HA; Montelione GT.  Protein Science. 2000, 9: 421 – 426. Solution NMR evidence for a cis Tyr-Ala peptide group in the structure of [Pro93Ala] bovine pancreatic ribonuclease A.  PMC2144552. Pubmed. 2. McDermott A; Polenova T; Bockmann A; Zilm KW; Paulson EK; Martin RW; Montelione GT. J. Biomol. NMR. 2000, 16:Continue reading “Publications 2000 & Prior”<\/span><\/a><\/p>\n","protected":false},"author":12,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-4478","page","type-page","status-publish","hentry","entry"],"_links":{"self":[{"href":"https:\/\/montelionelab.chem.rpi.edu\/index.php\/wp-json\/wp\/v2\/pages\/4478","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/montelionelab.chem.rpi.edu\/index.php\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/montelionelab.chem.rpi.edu\/index.php\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/montelionelab.chem.rpi.edu\/index.php\/wp-json\/wp\/v2\/users\/12"}],"replies":[{"embeddable":true,"href":"https:\/\/montelionelab.chem.rpi.edu\/index.php\/wp-json\/wp\/v2\/comments?post=4478"}],"version-history":[{"count":9,"href":"https:\/\/montelionelab.chem.rpi.edu\/index.php\/wp-json\/wp\/v2\/pages\/4478\/revisions"}],"predecessor-version":[{"id":4487,"href":"https:\/\/montelionelab.chem.rpi.edu\/index.php\/wp-json\/wp\/v2\/pages\/4478\/revisions\/4487"}],"wp:attachment":[{"href":"https:\/\/montelionelab.chem.rpi.edu\/index.php\/wp-json\/wp\/v2\/media?parent=4478"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}