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Gordon G. Hammes - Publications

Affiliations: 
1960-1965 Chemistry Massachusetts Institute of Technology, Cambridge, MA, United States 
 1965-1988 Chemistry and Chemical Biology Cornell University, Ithaca, NY, United States 
 1988-1991 Vice Chancellor University of California, Santa Barbara, Santa Barbara, CA, United States 
 1991-1998 Vice Chancellor Duke University, Durham, NC 
Area:
enzyme catalysis
Website:
http://www.asbmb.org/uploadedfiles/aboutus/asbmb_history/past_presidents/1990s/1994Hammes.html

129 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2012 Atlas R, Campbell P, Cozzarelli NR, Curfman G, Enquist L, Fink G, Flanagin A, Fletcher J, George E, Hammes G, Heyman D, Inglesby T, Kaplan S, Kennedy D, Krug J, et al. Uncensored exchange of scientific results (Proceedings of the National Academy of Sciences (2003) 100, 4, (1464) DOI: 10.1073/pnas.0630491100) Proceedings of the National Academy of Sciences of the United States of America. 109: 8352. DOI: 10.1073/Pnas.1206993109  0.481
2011 Hammes GG, Benkovic SJ, Hammes-Schiffer S. Flexibility, diversity, and cooperativity: pillars of enzyme catalysis. Biochemistry. 50: 10422-30. PMID 22029278 DOI: 10.1021/Bi201486F  0.399
2011 Alberty RA, Cornish-Bowden A, Goldberg RN, Hammes GG, Tipton K, Westerhoff HV. Recommendations for terminology and databases for biochemical thermodynamics. Biophysical Chemistry. 155: 89-103. PMID 21501921 DOI: 10.1016/J.Bpc.2011.03.007  0.53
2008 Hammes GG. How do enzymes really work? The Journal of Biological Chemistry. 283: 22337-46. PMID 18477561 DOI: 10.1074/Jbc.X800005200  0.333
2008 Benkovic SJ, Hammes GG, Hammes-Schiffer S. Free-energy landscape of enzyme catalysis. Biochemistry. 47: 3317-21. PMID 18298083 DOI: 10.1021/Bi800049Z  0.336
2007 Smiley RD, Collins TR, Hammes GG, Hsieh TS. Single-molecule measurements of the opening and closing of the DNA gate by eukaryotic topoisomerase II. Proceedings of the National Academy of Sciences of the United States of America. 104: 4840-5. PMID 17360343 DOI: 10.1073/Pnas.0700342104  0.318
2007 Hammes GG. SINGLE MOLECULE STUDIES OF ENZYME DYNAMICS AND MECHANISMS The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A90-B  0.319
2006 Smiley RD, Hammes GG. Single molecule studies of enzyme mechanisms. Chemical Reviews. 106: 3080-94. PMID 16895319 DOI: 10.1021/Cr0502955  0.33
2005 Antikainen NM, Smiley RD, Benkovic SJ, Hammes GG. Conformation coupled enzyme catalysis: single-molecule and transient kinetics investigation of dihydrofolate reductase. Biochemistry. 44: 16835-43. PMID 16363797 DOI: 10.1021/Bi051378I  0.388
2004 Zhang Z, Rajagopalan PT, Selzer T, Benkovic SJ, Hammes GG. Single-molecule and transient kinetics investigation of the interaction of dihydrofolate reductase with NADPH and dihydrofolate. Proceedings of the National Academy of Sciences of the United States of America. 101: 2764-9. PMID 14978269 DOI: 10.1073/Pnas.0400091101  0.4
2003 Atlas R, Campbell P, Cozzarelli NR, Curfman G, Enquist L, Fink G, Flanagin A, Fletcher J, George E, Hammes G, Heyman D, Inglesby T, Kaplan S, Kennedy D, Krug J, et al. Statement on scientific publication and security. Science (New York, N.Y.). 299: 1149. PMID 12595658 DOI: 10.1126/Science.299.5610.1149  0.461
2003 Atlas R, Campbell P, Cozzarelli NR, Curfman G, Enquist L, Fink G, Flanagin A, Fletcher J, George E, Hammes G, Heyman D, Inglesby T, Kaplan S, Kennedy D, Krug J, et al. Statement on the consideration of biodefence and biosecurity. Nature. 421: 771. PMID 12594463 DOI: 10.1038/Nature01479  0.472
2003 Atlas R, Campbell P, Cozzarelli NR, Curfman G, Enquist L, Fink G, Flanagin A, Fletcher J, George E, Hammes G, Heyman D, Inglesby T, Kaplan S, Kennedy D, Krug J, et al. Uncensored exchange of scientific results. Proceedings of the National Academy of Sciences of the United States of America. 100: 1464. PMID 12590129 DOI: 10.1073/pnas.0630491100  0.438
2002 Rajagopalan PT, Zhang Z, McCourt L, Dwyer M, Benkovic SJ, Hammes GG. Interaction of dihydrofolate reductase with methotrexate: ensemble and single-molecule kinetics. Proceedings of the National Academy of Sciences of the United States of America. 99: 13481-6. PMID 12359872 DOI: 10.1073/Pnas.172501499  0.389
2002 Hammes GG. Multiple conformational changes in enzyme catalysis. Biochemistry. 41: 8221-8. PMID 12081470 DOI: 10.1021/Bi0260839  0.383
1998 FASELLA P, HAMMES GG, VALLEE BL. Concerning the role of metals in enzymic transamination. Biochimica Et Biophysica Acta. 65: 142-3. PMID 13944491 DOI: 10.1016/0006-3002(62)90158-0  0.402
1998 FASELLA P, HAMMES GG. Studies of the enzyme hexokinase. IV. The role of sulfhydryl groups. Archives of Biochemistry and Biophysics. 100: 295-7. PMID 13944490 DOI: 10.1016/0003-9861(63)90075-4  0.318
1998 Hammes GG. A golden era for understanding enzyme mechanisms. Protein Science : a Publication of the Protein Society. 7: 799-802. PMID 9541414 DOI: 10.1002/Pro.5560070331  0.34
1995 Fierke CA, Hammes GG. Transient kinetic approaches to enzyme mechanisms. Methods in Enzymology. 249: 3-37. PMID 7791616 DOI: 10.1016/0076-6879(95)49029-9  0.392
1990 Musier-Forsyth KM, Hammes GG. Rotational dynamics of chloroplast ATP synthase in phospholipid vesicles. Biochemistry. 29: 3236-41. PMID 2159333 DOI: 10.1021/Bi00465A014  0.663
1990 Chang SI, Hammes GG. Structure and mechanism of action of a multifunctional enzyme: Fatty acid synthase Accounts of Chemical Research. 23: 363-369. DOI: 10.1021/Ar00179A003  0.526
1989 Chang SI, Hammes GG. Amino acid sequences of pyridoxal 5'-phosphate binding sites and fluorescence resonance energy transfer in chicken liver fatty acid synthase. Biochemistry. 28: 3781-8. PMID 2751995 DOI: 10.1021/Bi00435A023  0.557
1989 Holzer KP, Liu W, Hammes GG. Molecular cloning and sequencing of chicken liver fatty acid synthase cDNA. Proceedings of the National Academy of Sciences of the United States of America. 86: 4387-91. PMID 2734291 DOI: 10.1073/Pnas.86.12.4387  0.307
1989 Chang SI, Hammes GG. Homology analysis of the protein sequences of fatty acid synthases from chicken liver, rat mammary gland, and yeast. Proceedings of the National Academy of Sciences of the United States of America. 86: 8373-6. PMID 2682649 DOI: 10.1073/Pnas.86.21.8373  0.546
1989 Mitra B, Hammes GG. Structural map of the dicyclohexylcarbodiimide site of chloroplast coupling factor determined by resonance energy transfer. Biochemistry. 28: 3063-9. PMID 2525921 DOI: 10.1021/Bi00433A049  0.345
1988 Kashem MA, Hammes GG. Correlation of enzymatic activities and aggregation state in chicken liver fatty acid synthase. Biochimica Et Biophysica Acta. 956: 39-48. PMID 3408738 DOI: 10.1016/0167-4838(88)90295-6  0.365
1988 Chang SI, Hammes GG. Amino acid sequences of substrate-binding sites in chicken liver fatty acid synthase. Biochemistry. 27: 4753-60. PMID 3167014 DOI: 10.1021/Bi00413A026  0.534
1988 Musier KM, Hammes GG. Assessment of the number of nucleotide binding sites on chloroplast coupling factor 1 by the continuous variation method. Biochemistry. 27: 7015-20. PMID 2904277 DOI: 10.1021/Bi00418A052  0.345
1988 Leckband D, Hammes GG. Function of tightly bound nucleotides on membrane-bound chloroplast coupling factor. Biochemistry. 27: 3629-33. PMID 2900652 DOI: 10.1021/Bi00410A016  0.59
1988 Mitra B, Hammes GG. Characterization of three-subunit chloroplast coupling factor. Biochemistry. 27: 245-50. PMID 2894846 DOI: 10.1021/Bi00401A037  0.371
1987 Musier KM, Hammes GG. Rotation of nucleotide sites is not required for the enzymatic activity of chloroplast coupling factor 1. Biochemistry. 26: 5982-8. PMID 2891373 DOI: 10.1021/Bi00393A006  0.303
1987 Leckband D, Hammes GG. Interactions between nucleotide binding sites on chloroplast coupling factor during ATP hydrolysis. Biochemistry. 26: 2306-12. PMID 2887200 DOI: 10.1021/Bi00382A035  0.623
1987 Admon A, Hammes GG. Amino acid sequence of the nucleotide binding region of chloroplast coupling factor 1. Biochemistry. 26: 3193-7. PMID 2886150 DOI: 10.1021/Bi00385A038  0.352
1987 McCarty RE, Hammes GG. Molecular architecture of chloroplast coupling factor 1 Trends in Biochemical Sciences. 12: 234-237. DOI: 10.1016/0968-0004(87)90116-2  0.332
1986 Leanz GF, Hammes GG. Kinetic and nuclear magnetic resonance study of the interaction of NADP+ and NADPH with chicken liver fatty acid synthase. Biochemistry. 25: 5617-24. PMID 3535882 DOI: 10.1021/Bi00367A041  0.395
1986 Chang SI, Hammes GG. Interaction of spin-labeled nicotinamide adenine dinucleotide phosphate with chicken liver fatty acid synthase. Biochemistry. 25: 4661-8. PMID 3021196 DOI: 10.1021/Bi00364A031  0.566
1986 Schinkel JE, Hammes GG. Chloroplast coupling factor 1: dependence of rotational correlation time on polypeptide composition. Biochemistry. 25: 4066-71. PMID 2874828 DOI: 10.1021/Bi00362A012  0.358
1986 Krupinski J, Hammes GG. Steady-state ATP synthesis by bacteriorhodopsin and chloroplast coupling factor co-reconstituted into asolectin vesicles. Proceedings of the National Academy of Sciences of the United States of America. 83: 4233-7. PMID 2872676 DOI: 10.1073/Pnas.83.12.4233  0.306
1985 Krupinski J, Hammes GG. Phase-lifetime spectrophotometry of deoxycholate-purified bacteriorhodopsin reconstituted into asolectin vesicles. Biochemistry. 24: 6963-72. PMID 4074733 DOI: 10.1021/Bi00345A032  0.307
1985 Yuan ZY, Hammes GG. Elementary steps in the reaction mechanism of chicken liver fatty acid synthase. Acylation of specific binding sites. The Journal of Biological Chemistry. 260: 13532-8. PMID 4055747  0.312
1985 Anderson VE, Hammes GG. Distribution of reaction intermediates on chicken liver fatty acid synthase. Biochemistry. 24: 2147-54. PMID 3995008 DOI: 10.1021/Bi00330A007  0.566
1985 Cognet JA, Hammes GG. Elementary steps in the reaction mechanism of chicken liver fatty acid synthase: beta-ketoacyl reductase and enoyl reductase. Biochemistry. 24: 290-7. PMID 3978075 DOI: 10.1021/Bi00323A008  0.415
1985 Kambouris NG, Hammes GG. Investigation of nucleotide binding sites on chloroplast coupling factor 1 with 3'O-(4-benzoyl)benzoyl adenosine 5'-triphosphate. Proceedings of the National Academy of Sciences of the United States of America. 82: 1950-3. PMID 3856872 DOI: 10.1073/Pnas.82.7.1950  0.341
1985 Richter ML, Snyder B, McCarty RE, Hammes GG. Binding stoichiometry and structural mapping of the epsilon polypeptide of chloroplast coupling factor 1. Biochemistry. 24: 5755-63. PMID 2867774 DOI: 10.1021/Bi00342A011  0.406
1985 Snyder B, Hammes GG. Structural organization of chloroplast coupling factor. Biochemistry. 24: 2324-31. PMID 2859887 DOI: 10.1021/Bi00330A030  0.337
1984 Anderson VE, Hammes GG. Stereochemistry of the reactions catalyzed by chicken liver fatty acid synthase. Biochemistry. 23: 2088-94. PMID 6722137 DOI: 10.1021/Bi00304A033  0.561
1984 Waskiewicz DE, Hammes GG. Elementary steps in the reaction mechanism of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylation. Biochemistry. 23: 3136-43. PMID 6380583 DOI: 10.1021/Bi00309A005  0.344
1984 Snyder B, Hammes GG. Structural mapping of chloroplast coupling factor. Biochemistry. 23: 5787-95. PMID 6240988 DOI: 10.1021/Bi00319A018  0.334
1983 Cognet JA, Hammes GG. Elementary steps in the reaction mechanism of chicken liver fatty acid synthase: acetylation-deacetylation. Biochemistry. 22: 3002-7. PMID 6871181 DOI: 10.1021/Bi00281A033  0.4
1983 Anderson VE, Hammes GG. Fluorescent properties of pyrene bound at specific acylation sites of chicken liver fatty acid synthase. Biochemistry. 22: 2995-3001. PMID 6871180 DOI: 10.1021/Bi00281A032  0.624
1983 Cox BG, Hammes GG. Steady-state kinetic study of fatty acid synthase from chicken liver. Proceedings of the National Academy of Sciences of the United States of America. 80: 4233-7. PMID 6576333 DOI: 10.1073/Pnas.80.14.4233  0.365
1983 Cognet JA, Cox BG, Hammes GG. Elementary steps in the reaction mechanism of chicken liver fatty acid synthase: reduced nicotinamide adenine dinucleotide phosphate binding and formation and reduction of acetoacetyl-enzyme. Biochemistry. 22: 6281-7. PMID 6362722 DOI: 10.1021/Bi00295A037  0.431
1983 Cerione RA, McCarty RE, Hammes GG. Spatial relationships between specific sites on reconstituted chloroplast proton adenosinetriphosphatase and the phospholipid vesicle surface. Biochemistry. 22: 769-76. PMID 6220736 DOI: 10.1021/Bi00273A010  0.475
1983 Hammes GG. Mechanism of ATP synthesis and coupled proton transport: studies with purified chloroplast coupling factor Trends in Biochemical Sciences. 8: 131-134. DOI: 10.1016/0968-0004(83)90236-0  0.327
1982 Cardon JW, Hammes GG. Investigation of reduced nicotinamide adenine dinucleotide phosphate and acyl-binding sites on avian fatty acid synthase. Biochemistry. 21: 2863-70. PMID 7104298 DOI: 10.1021/Bi00541A009  0.419
1982 Waskiewicz DE, Hammes GG. Fluorescence polarization study of the alpha-ketoglutarate dehydrogenase complex from Escherichia coli. Biochemistry. 21: 6489-96. PMID 6758846 DOI: 10.1021/Bi00268A026  0.35
1982 Cerione RA, Hammes GG. Structural mapping of nucleotide binding sites on chloroplast coupling factor. Biochemistry. 21: 745-52. PMID 6462173 DOI: 10.1021/Bi00533A026  0.546
1982 Hammes GG. Unifying concept for the coupling between ion pumping and ATP hydrolysis or synthesis. Proceedings of the National Academy of Sciences of the United States of America. 79: 6881-4. PMID 6129623 DOI: 10.1073/Pnas.79.22.6881  0.367
1981 Akiyama SK, Hammes GG. Elementary steps in the reaction mechanism of pyruvate dehydrogenase multienzyme complex from Escherichia coli: kinetics of flavin reduction. Biochemistry. 20: 1491-7. PMID 7013795 DOI: 10.1021/Bi00509A013  0.327
1981 Bruist MF, Hammes GG. Further characterization of nucleotide binding sites on chloroplast coupling factor one. Biochemistry. 20: 6298-305. PMID 6458326 DOI: 10.1021/Bi00525A003  0.367
1981 Cerione RA, Hammes GG. Nucleotide interactions with the dicyclohexylcarbodiimide-sensitive adenosinetriphosphatase from spinach chloroplasts. Biochemistry. 20: 3359-65. PMID 6455155 DOI: 10.1021/Bi00515A008  0.594
1980 Akiyama SK, Hammes GG. Elementary steps in the reaction mechanism of the pyruvate dehydrogenase multienzyme complex from Escherichia coli: kinetics of acetylation and deacetylation. Biochemistry. 19: 4208-13. PMID 6998493 DOI: 10.1021/Bi00559A011  0.398
1980 Craig DW, Hammes GG. Structural mapping of rabbit muscle phosphofructokinase. Distance between the adenosine cyclic 3',5'-phosphate binding site and a reactive sulfhydryl group. Biochemistry. 19: 330-4. PMID 6243478 DOI: 10.1021/Bi00543A013  0.364
1979 Baird BA, Hammes GG. Structure of oxidative- and photo-phosphorylation coupling factor complexes. Biochimica Et Biophysica Acta. 549: 31-53. PMID 157776 DOI: 10.1016/0304-4173(79)90017-X  0.506
1979 Carlier MF, Holowka DA, Hammes GG. Interaction of photoreactive and fluorescent nucleotides with chloroplast coupling factor 1. Biochemistry. 18: 3452-7. PMID 157773  0.491
1979 Baird BA, Pick U, Hammes GG. Structural investigation of reconstituted chloroplast ATPase with fluorescence measurements. The Journal of Biological Chemistry. 254: 3818-25. PMID 155694  0.469
1978 Hahn LH, Hammes GG. Structural mapping of aspartate transcarbamoylase by fluorescence energy-transfer measurements: determination of the distance between catalytic sites of different subunits. Biochemistry. 17: 2423-9. PMID 678521 DOI: 10.1021/Bi00605A027  0.306
1978 Angelides KJ, Hammes GG. Mechanism of action of the pyruvate dehydrogenase multienzyme complex from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 75: 4877-80. PMID 368802 DOI: 10.1073/Pnas.75.10.4877  0.349
1977 Baird BA, Hammes GG. Chemical cross-linking studies of beef heart mitochondrial coupling factor 1. The Journal of Biological Chemistry. 252: 4743-8. PMID 873913  0.439
1977 Shepherd GB, Hammes GG. Fluorescence energy transfer measurements in the pyruvate dehydrogenase multienzyme complex from Escherichia coli with chemically modified lipoic acid. Biochemistry. 16: 5234-41. PMID 336083 DOI: 10.1021/Bi00643A012  0.31
1977 Papadakis N, Hammes GG. Fluorescent derivatives of the pyruvate dehydrogenase component of the Escherichia coli pyruvate dehydrogenase complex. Biochemistry. 16: 1890-6. PMID 192277 DOI: 10.1021/Bi00628A020  0.418
1977 Holowka DA, Hammes GG. Chemical modification and fluorescence studies of chloroplast coupling factor. Biochemistry. 16: 5538-45. PMID 144521 DOI: 10.1021/Bi00644A023  0.538
1976 Cantley LC, Hammes GG. Investigation of quercetin binding sites on chloroplast coupling factor 1. Biochemistry. 15: 1-8. PMID 1247500 DOI: 10.1021/Bi00646A001  0.501
1976 Shepherd GB, Hammes GG. Fluorescence energy transfer measurements between ligand binding sites of the pyruvate dehydrogenase multienzyme complex. Biochemistry. 15: 311-7. PMID 764864 DOI: 10.1021/Bi00647A011  0.415
1976 Baird BA, Hammes GG. Chemical cross-linking studies of chloroplast coupling factor 1. The Journal of Biological Chemistry. 251: 6953-62. PMID 136444  0.465
1976 Parr GR, Hammes GG. A kinetic study of the subunit dissociation and reassembly of rabbit muscle phosphofructokinase. Biochemistry. 15: 857-62. PMID 129154 DOI: 10.1021/Bi00649A020  0.377
1976 Cantley LC, Hammes GG. Characterization of sulfhydryl groups on chloroplast coupling factor 1 exposed by heat activation. Biochemistry. 15: 9-14. PMID 129152 DOI: 10.1021/Bi00646A002  0.5
1976 Hammes GG, Rodbell M. Simple model for hormone-activated adenylate cyclase systems. Proceedings of the National Academy of Sciences of the United States of America. 73: 1189-92. PMID 4796 DOI: 10.1073/Pnas.73.4.1189  0.332
1975 Cantley LC, Hammes GG. Fluorescence energy transfer between ligand binding sites on chloroplast coupling factor 1. Biochemistry. 14: 2976-81. PMID 1148188 DOI: 10.1021/Bi00684A028  0.492
1975 Cantley LC, Hammes GG. Characterization of nucleotide binding sites on chloroplast coupling factor 1. Biochemistry. 14: 2968-75. PMID 1148187 DOI: 10.1021/Bi00684A027  0.521
1975 Matsumoto S, Hammes GG. Fluorescence energy transfer between ligand binding sites on aspartate transcarbamylase Biochemistry. 14: 214-224. PMID 1091284 DOI: 10.1021/Bi00673A004  0.356
1975 Fan S, Harrison LW, Hammes GG. Nuclear magnetic resonance study of ligand binding to Mn-aspartate transcarbamylase. Biochemistry. 14: 2219-24. PMID 807235 DOI: 10.1021/Bi00681A027  0.393
1975 Koren R, Hammes GG. Interaction of reduced nicotinamide adenine dinucleotide with beef heart s-malate dehydrogenase Biochemistry. 14: 1021-1025. PMID 164884 DOI: 10.1021/Bi00676A021  0.411
1975 Parr GR, Hammes GG. Subunit dissociation and unfolding of rabbit muscle phosphofructokinase by guanidine hydrochloride Biochemistry. 14: 1600-1605. PMID 123759 DOI: 10.1021/Bi00679A009  0.346
1975 Hill DE, Hammes GG. An equilibrium binding study of the interaction of fructose 6-phosphate and fructose 1,6-bisphosphate with rabbit muscle phosphofructokinase Biochemistry. 14: 203-213. PMID 123467 DOI: 10.1021/Bi00673A003  0.383
1974 Moe OA, Hammes GG. A study of the binding of thiamine diphosphate and thiochrome diphosphate to the pyruvate dehydrogenase multienzyme complex Biochemistry. 13: 2547-2552. PMID 4598732 DOI: 10.1021/Bi00709A011  0.334
1974 Hammes GG, Wu CW. Kinetics of allosteric enzymes Annual Review of Biophysics and Bioengineering. 3: 1-33. PMID 4371650  0.542
1974 Grover AK, Hammes GG. Affinity chromatography of β-hydroxybutyrate dehydrogenase on NAD and hydrophobic chain derivatives of sepharose Bba - Biomembranes. 356: 309-318. PMID 4367726 DOI: 10.1016/0005-2736(74)90271-5  0.332
1974 Moe OA, Lerner DA, Hammes GG. Fluorescence energy transfer between the thiamine diphosphate and flavine adenine dinucleotide binding sites on the pyruvate dehydrogenase multienzyme complex Biochemistry. 13: 2552-2557. PMID 4364834 DOI: 10.1021/Bi00709A012  0.342
1974 Hammes GG. Elementary steps in enzyme catalysis and regulation Pure and Applied Chemistry. 40: 525-548. DOI: 10.1351/Pac197440040525  0.417
1973 Wu CW, Hammes GG. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with an adenosine 5′-triphosphate analog Biochemistry. 12: 1400-1408. PMID 4572360 DOI: 10.1021/Bi00731A021  0.628
1973 Harrison LW, Hammes GG. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with cytidine 5′-triphosphate Biochemistry. 12: 1395-1400. PMID 4572359 DOI: 10.1021/Bi00731A020  0.426
1973 Matsumoto S, Hammes GG. An equilibrium binding study of the interaction of aspartate transcarbamylase with cytidine 5'-triphosphate and adenosine 5'-triphosphate. Biochemistry. 12: 1388-94. PMID 4572358 DOI: 10.1021/Bi00731A019  0.312
1973 Cantley LC, Hammes GG. Activation of beef heart mitochondrial adenosine triphosphatase by 2,4-dinitrophenol. Biochemistry. 12: 4900-4. PMID 4271561 DOI: 10.1021/Bi00748A014  0.395
1973 Tondre C, Hammes GG. A kinetic study of the binding of an ADP fluorescent analog to mitochondrial ATPase. Biochimica Et Biophysica Acta. 314: 245-9. PMID 4270537 DOI: 10.1016/0005-2728(73)90139-4  0.376
1972 Hammes GG, Hilborn DA. Steady state kinetics of soluble and membrane-bound mitochondrial ATPase. Biochimica Et Biophysica Acta. 233: 580-90. PMID 4255902 DOI: 10.1016/0005-2736(71)90156-8  0.372
1971 Hammes GG, Tallman DE. A nuclear magnetic resonance study of the interaction of l-epinephrine with phospholipid vesicles Bba - Biomembranes. 233: 17-25. PMID 5103878 DOI: 10.1016/0005-2736(71)90353-1  0.54
1971 Hammes GG, Wu CW. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with carbamyl phosphate Biochemistry. 10: 2150-2156. PMID 4935107 DOI: 10.1021/Bi00787A030  0.601
1971 Hammes GG, Wu CW. Regulation of enzyme activity Science. 172: 1205-1211. PMID 4930512 DOI: 10.1126/Science.172.3989.1205  0.562
1971 Hammes GG, Wu CW. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with aspartate analogs Biochemistry. 10: 1051-1057. PMID 4927804 DOI: 10.1021/Bi00782A018  0.604
1971 Hammes GG, Porter RW, Stark GR. Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate. Biochemistry. 10: 1046-50. PMID 4927803 DOI: 10.1021/Bi00782A017  0.305
1970 Hammes GG, Porter RW, Wu CW. Determination of the number of regulatory and catalytic sites on aspartate transcarbamylase. Biochemistry. 9: 2992-4. PMID 5474800 DOI: 10.1021/Bi00817A009  0.532
1970 Hammes GG, Tallman DE. Application of the temperature-jump technique to the study of phospholipid dispersions Journal of the American Chemical Society. 92: 6042-6046. PMID 5460540 DOI: 10.1021/Ja00723A038  0.562
1970 Hammes GG, Simplicio J. Relaxation spectra of pyruvate kinase. Biochimica Et Biophysica Acta. 212: 428-33. PMID 5456993 DOI: 10.1016/0005-2744(70)90248-2  0.389
1970 Eckfeldt J, Hammes GG, Mohr SC, Wu CW. Relaxation spectra of aspartate transcarbamylase. I. Interaction of 5-bromocytidine triphosphate with native enzyme and regulatory subunit Biochemistry. 9: 3353-3362. PMID 4941833 DOI: 10.1021/Bi00819A010  0.621
1970 Faeder EJ, Hammes GG. Kinetic studies of tryptophan synthetase. Interaction of substrates with the B subunit. Biochemistry. 9: 4043-9. PMID 4917898 DOI: 10.1021/Bi00823A003  0.308
1970 Hammes GG, Schimmel PR. 2 Rapid Reactions and Transient States The Enzymes. 2: 67-114. DOI: 10.1016/S1874-6047(08)60181-X  0.33
1969 Hammes GG, Hurst JK. Relaxation spectra of adenosine triphosphate-creatine phosphotransferase. Biochemistry. 8: 1083-94. PMID 5813732 DOI: 10.1021/Bi00831A040  0.567
1968 Hammes GG, Pace CN. Ultrasonic absorption measurements in aqueous solutions of glycine, diglycine, and triglycine. The Journal of Physical Chemistry. 72: 2227-30. PMID 5650147 DOI: 10.1021/j100852a060  0.422
1968 Anderson DG, Hammes GG, Walz FG. Binding of phosphate ligands to ribonuclease A Biochemistry. 7: 1637-1645. PMID 4297049 DOI: 10.1021/Bi00845A004  0.32
1967 Hammes GG, Schimmel PR. Relaxation spectra of enzymatic reactions. The Journal of Physical Chemistry. 71: 917-23. PMID 6045206 DOI: 10.1021/J100863A023  0.599
1966 Erman JE, Hammes GG. Relaxation spectra of ribonuclease. V. The interaction of ribonuclease with cytidylyl-3′:5′-cytidine Journal of the American Chemical Society. 88: 5614-5617. PMID 5980178 DOI: 10.1021/Ja00975A047  0.377
1966 Erman JE, Hammes GG. Relaxation spectra of ribonuclease. IV. The interaction of ribonuclease with cytidine 2′:3′-cyclic phosphate Journal of the American Chemical Society. 88: 5607-5614. PMID 5980177 DOI: 10.1021/Ja00975A046  0.401
1965 Fasella P, Hammes GG, Schimmel PR. A Sephadex dialysis method of determining small molecule-macromolecule binding constants. Biochimica Et Biophysica Acta. 103: 708-10. PMID 5859855 DOI: 10.1016/0005-2787(65)90094-8  0.588
1965 Hammes GG, Schimmel PR. Equilibrium measurements of the binding of cytidine 3'-phosphate to ribonuclease. Journal of the American Chemical Society. 87: 4665-9. PMID 5844451 DOI: 10.1021/Ja00949A001  0.602
1965 Cathou RE, Hammes GG, Schimmel PR. Optical rotatory dispersion of ribonuclease and ribonuclease--nucleotide complexes. Biochemistry. 4: 2687-90. PMID 4286548 DOI: 10.1021/Bi00888A018  0.557
1964 Hammes GG. Mechanism of Enzyme Catalysis Nature. 204: 342-343. PMID 14228866 DOI: 10.1038/204342A0  0.354
1964 Cathou RE, Hammes GG. Relaxation Spectra of Ribonuclease. I. The Interaction of Ribonuclease with Cytidine 3′-Phosphate Journal of the American Chemical Society. 86: 3240-3245. DOI: 10.1021/Ja01070A008  0.398
1963 EIGEN M, HAMMES GG. ELEMENTARY STEPS IN ENZYME REACTIONS (AS STUDIED BY RELAXATION SPECTROMETRY). Advances in Enzymology and Related Areas of Molecular Biology. 25: 1-38. PMID 14149678  0.553
1962 Hammes GG, Kochavi D. Studies of the Enzyme Hexokinase. II. Kinetic Inhibition by Products Journal of the American Chemical Society. 84: 2073-2076. DOI: 10.1021/Ja00870A013  0.314
1962 Hammes GG, Kochavi D. Studies of the Enzyme Hexokinase. I. Steady State Kinetics at pH 8 Journal of the American Chemical Society. 84: 2069-2073. DOI: 10.1021/Ja00870A012  0.325
1961 Eigen M, Hammes GG. Kinetic Studies of ADP Reactions with the Temperature Jump Method—Corrections Journal of the American Chemical Society. 83: 2786-2786. DOI: 10.1021/Ja01473A056  0.543
1960 DIEBLER H, EIGEN M, HAMMES GG. [Relaxation spectrometric studies of fast reactions of ATP in aqueous solution]. Zeitschrift FüR Naturforschung. Teil B: Chemie, Biochemie, Biophysik, Biologie. 15: 554-60. PMID 13722730 DOI: 10.1515/Znb-1960-0903  0.55
1960 Diebler H, Eigen M, Hammes GG. Relaxations-spektrometrische Untersuchungen schneller Reaktionen von ATP in wässeriger Lösung Zeitschrift Fur Naturforschung - Section B Journal of Chemical Sciences. 15: 554-560. DOI: 10.1515/znb-1960-0903  0.506
1960 Eigen M, Hammes GG. KINETIC STUDIES OF ADP REACTIONS WITH THE TEMPERATURE JUMP METHOD Journal of the American Chemical Society. 82: 5951-5952. DOI: 10.1021/Ja01507A041  0.542
1960 Figen M, Hammes GG, Kustin K. FAST REACTIONS OF IMIDAZOLE STUDIED WITH RELAXATION SPECTROMETRY Journal of the American Chemical Society. 82: 3482-3483. DOI: 10.1021/Ja01498A063  0.518
1960 Hammes GG, Alberty RA. The Relaxation Spectra of Simple Enzymatic Mechanisms1,2 Journal of the American Chemical Society. 82: 1564-1569. DOI: 10.1021/Ja01492A012  0.521
1959 Hammes GG, Alberty RA. The influence of the net protein charge on the rate of formation of enzyme-substrate complexes Journal of Physical Chemistry. 63: 274-279. DOI: 10.1021/J150572A034  0.55
1958 Alberty RA, Hammes GG. Application of the theory of diffusion-controlled reactions to enzyme kinetics Journal of Physical Chemistry. 62: 154-159. DOI: 10.1021/J150560A005  0.54
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