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John Anthony Schellman

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405:. He clarified the foundations of the subjects he studied, especially of circular dichroism and the energetics of protein folding. In 1962 John and his student Patrick Oriel found that the n-pi* transition of the peptide group is responsible for the Cotton effect that is used to measure α-helix formation in ORD studies. (In CD studies, the n-pi* transition is responsible for the 220 nm CD band that is used to measure α-helix content.) ...In the 1970s the study of protein mutants became an important approach to the protein folding problem and John and his coworkers developed methods of analyzing the properties of mutant proteins. John's methods were widely used, both in equilibrium studies of mutational effects on protein stability and in kinetic studies of how mutations affect the rates of protein folding. 374:, and they married in 1954. (She developed the "Schellman motif", on α-helix termination in proteins by a characteristic sequence.) According to Baldwin and von Hippel, "Their ORD results were published in a magnum opus (seven papers on ten proteins) in 1958, after they had left the Carlsberg Lab." 358:
in water?" and "concluded from his study that a single α-helix should have borderline stability in water, and that helix length should be a critical variable in determining helix stability". Third, with Harrington he investigated how a neighboring tertiary structure might affect the stability of an
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Colleague Henryk Eisenberg wrote that Schellman's studies were strong "in the examination of biological macromolecules, proteins and nucleic acids, in terms of their interactions with large and small molecules, solvents and solutes, sometimes in 'crowded' environments, mimicking biological media."
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upon Schellman's retirement in 2002, Hong Qian, James Hofrichter, and Robert L. Baldwin wrote that his scientific career hasd "paralleled the development of biophysical chemistry." Referring to his "landmark paper on the stability of the α-helix in 1955", as well as his research and teaching, they
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Eisenberg said Shellman's contributions included, "fluctuations and linkage relations in macromolecular solutions w25x, a simple model for solvation in mixed solvents w26x, the relation between the free energy of interaction and binding w27x and the thermodynamics of solvent exchange w28x."
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and co-workers determined the structure of the first protein (sperm whale myoglobin) at 0.6 nm resolution, could α-helices begin to be seen. So John's paper was on the cutting edge, to put it mildly. His was also the first modern paper on the energetics of
426:(yes, including physics, mathematics and spectroscopy!) into the center stage of biochemistry and molecular biology. An essential characteristic of John's work is the integration of theoretical analysis with experimental measurement." 1001:
For the application of rigorous physical theory and the development of novel experimental techniques to increase our understanding of the structure and behavior of biological macromolecules, especially proteins and nucleic
390:, where he held joint appointments as an associate professor in the departments of Chemistry and the Institute of Molecular Biology, and she was an adjunct professor. He was promoted to professor in 1963, and he retired as 294:. He and post-doc Bill Harrington were the first to show "protein unfolding transitions were fast and reversible and thus were reactions suitable for quantitative physico-chemical analysis", initiating reversible 359:α-helix, learning "that indeed tertiary structure and other stabilizing elements (such as inter-chain S-S bonds) might be critical in stabilizing the individual secondary structure elements of 1478: 203:
in taverns for extra cash. Schellman especially enjoyed high school chemistry, and reportedly came close to burning down the house when a basement experiment caught fire.
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The son of John A. and Margaret Mary (née Mason) Schellman, John Anthony Schellman was born in Philadelphia on October 24, 1924. His father, a
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Schellman, C. and J. A. Schellman. 1958. VII. Optical rotation and protein configuration. C. R.trav. lab. Carlsberg Ser. Chim. 30:463-500.
928:"Evidence for the instability of hydrogen-bonded peptide structures in water, based on studies of ribonuclease and oxidized ribonuclease. 338:'s landmark paper on the energetic importance of burying non-polar side chains in the interior of proteins appeared 4 years later in 1959. 263: 371: 282:. Although he did not find that work interesting, he was still interested in proteins, and transferred his postdoctoral fellowship to 1534: 1016: 325:
had proposed that the α-helix should be a major structural unit in proteins, but no one had yet seen an α-helix. Only in 1958, when
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After high school, his family's limited finances did not allow him to attend college. Schellman worked in a factory, then in the
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Schellman's ensuing research led to three important developments. First, he "derived an equation to analyze how the number of
1145: 401:...John dug deeper into the problems he had opened up at the Carlsberg Lab and began to analyze the physical properties of 1084: 978: 968: 419: 291: 267: 990: 172: 350:
molecules in water should change when a concentrated urea solution is diluted", yielding measurements suggesting "the
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In 1955 John Schellman wrote a paper estimating the stability of the α-helix in aqueous solution. Four years earlier
218:, because of poor eyesight he was deemed unfit for combat, and he was assigned to the Army's medical laboratory at 996: 962: 180: 237:, in just two years, in 1948. He earned an M.A. in 1949 and a Ph.D. in Theoretical Chemistry in 1951, both at 383: 207: 974: 200: 164: 1435: 1395: 1361: 1280: 1206: 1514: 1509: 804: 514: 453: 387: 367: 283: 238: 168: 124: 422:, with his wife Charlotte. They wrote he was "instrumental in bringing the rigor and methodology of 1035: 1028: 176: 80: 1324: 1162: 1056: 879: 851: 836: 691: 663: 648: 597: 546: 423: 1460: 1452: 1436:"Focal contributions to molecular biophysics and structural biology: a personal view. Part II" 1412: 1305: 1297: 1235: 1227: 943: 914: 871: 828: 820: 777: 769: 734: 726: 683: 640: 632: 589: 581: 538: 530: 487: 469: 230: 211: 119: 1444: 1404: 1370: 1289: 1219: 1190:
Directory of Graduate Research, American Chemical Society Committee on Professional Training
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H-bond should be marginally stable in water". Second, he asked, "How stable is a single
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laboratory, a lab doing applied research. He also took a chemistry class after work at
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1986 Chalmers 150th Anniversary Professorship, Chalmers University, Gothenburg, Sweden
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Chakrabartty, Avijit; Schellman, John A.; Baldwin, Robert L. (June 1991).
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Of Schellman's work at Oregon, Robert Baldwin and Peter von Hippel wrote,
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In 1956 Schellman joined the faculty of the Chemistry Department of the
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Qian, Hong; Hofrichter, James; Baldwin, Robert L (December 10, 2002).
816: 526: 131: 503:"Large differences in the helix propensities of alanine and glycine" 195:, lost his position when the shop where he worked closed during the 275: 347: 1288:. Special issue in honour of John A Schellman. 101–102: 9–13. 402: 1057:"Philadelphia, Pennsylvania, U.S., Marriage Index, 1885-1951" 750:"DNA condensation with polyamines: I. Spectroscopic studies" 707:"DNA condensation with polyamines: I. Spectroscopic studies" 366:
In Copenhagen Schellman met Frances "Charlotte" Green, of
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Gosule, Leonard C.; Schellman, John A. (January 1976).
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Gosule, Leonard C.; Schellman, John A. (May 25, 1978).
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Gosule, Leonard C.; Schellman, John A. (May 25, 1978).
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Becktel, Wayne J.; Schellman, John A. (November 1987).
163:(October 24, 1924–December 16, 2014) was an American 930:
Comptes Rendus des Travaux du Laboratoire Carlsberg.
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asa major field of work. Schellman also developed "
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(1956). 418:commented on his work in the tradition of 36: 20: 1325:"U.S., Obituary Collection, 1930-Current" 1144:Baldwin, Robert L.; von Hippel, Peter H. 895:"Circular dichroism and optical rotation" 481: 1525:Fellows of the American Physical Society 1281:"John Schellman and his scientific work" 16:American biophysical chemist (1924–2014) 1433:Eisenberg, Henryk (December 10, 2002). 1278:Baldwin, Robert L (December 10, 2002). 1047: 386:. In 1958 the Schellmans moved to the 1428: 1426: 1388: 1386: 1384: 1139: 1137: 1135: 1133: 1131: 1129: 1127: 1011:American Academy of Arts and Sciences 7: 1242:– via Elsevier Science Direct. 1177:– via Elsevier Science Direct. 1125: 1123: 1121: 1119: 1117: 1115: 1113: 1111: 1109: 1107: 123:M.A., 1949 and Ph.D., 1951, both at 1085:"1930 United States Federal Census" 893:Schellman, John A. (June 1, 1975). 440:Schellman, John A. (July 1, 2003). 1193:. American Chemical Society. 1974. 977:, Department of Chemical Physics, 310:secondary structures of proteins. 14: 1204:Di Cera, Enrico (April 1, 2015). 611:Schellman, John A. (April 1987). 272:University of Utah Medical School 229:benefits and completed an A.B at 1540:University of Minnesota faculty 1169:. 101–102: 1–5. December 2002. 967:1962–1967 BBC Study Section of 850:Schellman, John A. (May 1975). 662:Schellman, John A. (May 1978). 241:. His dissertation was titled, 1207:"John A. Schellman, 1924–2014" 1: 1449:10.1016/S0301-4622(02)00164-3 1409:10.1016/S0301-4622(02)00185-0 1375:10.1016/S0301-4622(02)00186-2 1294:10.1016/S0301-4622(02)00194-1 1175:10.1016/S0301-4622(02)00186-2 466:10.1016/S0006-3495(03)74459-2 1545:University of Oregon faculty 991:National Academy of Sciences 766:10.1016/0022-2836(78)90366-2 754:Journal of Molecular Biology 723:10.1016/0022-2836(78)90366-2 711:Journal of Molecular Biology 173:National Academy of Sciences 1530:Princeton University alumni 300:optical rotatory dispersion 1561: 1359:Shellman, John A. (2002). 868:10.1002/bip.1975.360140509 680:10.1002/bip.1978.360170515 562:"Protein stability curves" 370:, who was a post-doc from 270:, with Leo Samuels at the 264:U.S. Public Health Service 1224:10.1016/j.bpc.2014.12.004 1027:1990 Honorary Doctorate, 1015:1983 Honorary Doctorate, 997:American Physical Society 313:Robert L. Baldwin wrote, 181:American Physical Society 154: 105: 100:biological macromolecules 35: 1535:Temple University alumni 1146:"John Anthony Schellman" 852:"Macromolecular binding" 258:Post-doctoral fellowship 187:Early life and education 950:– via Europe PMC. 384:University of Minnesota 1520:American biophysicists 664:"Solvent denaturation" 407: 340: 208:Philadelphia Gas Works 161:John Anthony Schellman 96:optical spectroscopies 25:John Anthony Schellman 1441:Biophysical Chemistry 1401:Biophysical Chemistry 1377:– via Elsevier. 1367:Biophysical Chemistry 1286:Biophysical Chemistry 1212:Biophysical Chemistry 1167:Biophysical Chemistry 629:10.1002/bip.360260408 578:10.1002/bip.360261104 434:Selected publications 415:Biophysical Chemistry 413:issue of the journal 1479:"APS Fellow Archive" 989:1982 Elected to the 388:University of Oregon 368:St. Joseph, Missouri 292:Kaj Linderstrøm-Lang 284:Carlsberg Laboratory 239:Princeton University 220:Walter Reed Hospital 169:University of Oregon 125:Princeton University 1163:"John A. Schellman" 1036:Biophysical Society 1029:University of Padua 1017:Chalmers University 911:10.1021/cr60295a004 809:1976Natur.259..333G 519:1991Natur.351..586C 458:2003BpJ....85..108S 446:Biophysical Journal 288:Copenhagen, Denmark 245:and was advised by 177:Biophysical Society 165:biophysical chemist 110:Academic background 81:Biophysical chemist 1443:. 101–102: 15–27. 1362:"Curriculum vitae" 979:Weizmann Institute 424:physical chemistry 392:professor emeritus 302:(ORD)" to measure 171:, a member of the 29:Professor emeritus 975:Guggenheim Fellow 803:(5541): 333–335. 572:(11): 1859–1877. 513:(6327): 586–588. 378:Faculty positions 361:globular proteins 231:Temple University 214:. Drafted during 212:Temple University 158: 157: 120:Temple University 62:December 16, 2014 1552: 1494: 1493: 1491: 1489: 1475: 1469: 1468: 1438: 1430: 1421: 1420: 1403:. 101–102: 7–8. 1398: 1390: 1379: 1378: 1369:. 101–102: 1–5. 1364: 1356: 1350: 1347: 1341: 1340: 1338: 1336: 1330:www.ancestry.com 1327: 1320: 1314: 1313: 1283: 1275: 1269: 1268: 1266: 1264: 1250: 1244: 1243: 1209: 1201: 1195: 1194: 1185: 1179: 1178: 1159: 1153: 1152: 1150: 1141: 1102: 1101: 1099: 1097: 1090:www.ancestry.com 1087: 1080: 1074: 1073: 1071: 1069: 1059: 1052: 951: 922: 899:Chemical Reviews 887: 844: 817:10.1038/259333a0 785: 742: 699: 674:(5): 1305–1322. 656: 605: 554: 527:10.1038/351586a0 495: 485: 420:Linderstrøm-Lang 280:steroid hormones 197:Great Depression 145:Doctoral advisor 65: 48:October 24, 1924 40: 21: 1560: 1559: 1555: 1554: 1553: 1551: 1550: 1549: 1500: 1499: 1498: 1497: 1487: 1485: 1477: 1476: 1472: 1432: 1431: 1424: 1392: 1391: 1382: 1358: 1357: 1353: 1348: 1344: 1334: 1332: 1322: 1321: 1317: 1277: 1276: 1272: 1262: 1260: 1252: 1251: 1247: 1203: 1202: 1198: 1187: 1186: 1182: 1161: 1160: 1156: 1148: 1143: 1142: 1105: 1095: 1093: 1082: 1081: 1077: 1067: 1065: 1054: 1053: 1049: 1044: 983:Rehovot, Israel 958: 925: 892: 862:(5): 999–1018. 849: 790: 747: 704: 661: 610: 559: 500: 439: 436: 380: 332:protein folding 296:protein-folding 260: 255: 247:Walter Kauzmann 189: 179:Fellow, and an 149:Walter Kauzmann 122: 72: 67: 63: 54: 49: 31: 26: 17: 12: 11: 5: 1558: 1556: 1548: 1547: 1542: 1537: 1532: 1527: 1522: 1517: 1512: 1502: 1501: 1496: 1495: 1470: 1422: 1380: 1351: 1342: 1315: 1270: 1245: 1196: 1180: 1154: 1103: 1075: 1046: 1045: 1043: 1040: 1039: 1038: 1032: 1025: 1021: 1020: 1013: 1006: 1005: 999:Fellow, cited 993: 986: 985: 971: 965: 957: 956:Awards, honors 954: 953: 952: 936:Serie Chimique 923: 905:(3): 323–331. 889: 888: 846: 845: 787: 786: 760:(3): 311–326. 744: 743: 717:(3): 311–326. 701: 700: 658: 657: 623:(4): 549–559. 607: 606: 556: 555: 497: 496: 452:(1): 108–125. 435: 432: 379: 376: 259: 256: 254: 251: 235:Phi Beta Kappa 188: 185: 156: 155: 152: 151: 146: 142: 141: 134: 128: 127: 116: 112: 111: 107: 106: 103: 102: 92:Thermodynamics 89: 88:Known for 85: 84: 78: 74: 73: 70:Eugene, Oregon 68: 66:(aged 90) 60: 56: 55: 50: 46: 42: 41: 33: 32: 27: 24: 15: 13: 10: 9: 6: 4: 3: 2: 1557: 1546: 1543: 1541: 1538: 1536: 1533: 1531: 1528: 1526: 1523: 1521: 1518: 1516: 1513: 1511: 1508: 1507: 1505: 1484: 1480: 1474: 1471: 1466: 1462: 1458: 1454: 1450: 1446: 1442: 1437: 1429: 1427: 1423: 1418: 1414: 1410: 1406: 1402: 1397: 1389: 1387: 1385: 1381: 1376: 1372: 1368: 1363: 1355: 1352: 1346: 1343: 1331: 1326: 1319: 1316: 1311: 1307: 1303: 1299: 1295: 1291: 1287: 1282: 1274: 1271: 1259: 1255: 1249: 1246: 1241: 1237: 1233: 1229: 1225: 1221: 1217: 1213: 1208: 1200: 1197: 1192: 1191: 1184: 1181: 1176: 1172: 1168: 1164: 1158: 1155: 1147: 1140: 1138: 1136: 1134: 1132: 1130: 1128: 1126: 1124: 1122: 1120: 1118: 1116: 1114: 1112: 1110: 1108: 1104: 1091: 1086: 1079: 1076: 1063: 1058: 1051: 1048: 1041: 1037: 1034:2001 Fellow, 1033: 1030: 1026: 1023: 1022: 1018: 1014: 1012: 1009:1983 Member, 1008: 1007: 1003: 998: 994: 992: 988: 987: 984: 980: 976: 972: 970: 966: 964: 960: 959: 955: 949: 945: 941: 937: 933: 931: 924: 920: 916: 912: 908: 904: 900: 896: 891: 890: 885: 881: 877: 873: 869: 865: 861: 857: 853: 848: 847: 842: 838: 834: 830: 826: 822: 818: 814: 810: 806: 802: 798: 794: 789: 788: 783: 779: 775: 771: 767: 763: 759: 755: 751: 746: 745: 740: 736: 732: 728: 724: 720: 716: 712: 708: 703: 702: 697: 693: 689: 685: 681: 677: 673: 669: 665: 660: 659: 654: 650: 646: 642: 638: 634: 630: 626: 622: 618: 614: 609: 608: 603: 599: 595: 591: 587: 583: 579: 575: 571: 567: 563: 558: 557: 552: 548: 544: 540: 536: 532: 528: 524: 520: 516: 512: 508: 504: 499: 498: 493: 489: 484: 479: 475: 471: 467: 463: 459: 455: 451: 447: 443: 438: 437: 433: 431: 427: 425: 421: 416: 412: 409:In a special 406: 404: 398: 395: 393: 389: 385: 377: 375: 373: 369: 364: 362: 357: 353: 349: 346:made between 345: 339: 337: 333: 328: 324: 320: 314: 311: 309: 305: 301: 297: 293: 289: 285: 281: 277: 273: 269: 265: 257: 252: 250: 248: 244: 240: 236: 232: 228: 223: 221: 217: 213: 209: 204: 202: 201:Irish ballads 198: 194: 186: 184: 182: 178: 174: 170: 166: 162: 153: 150: 147: 143: 140: 139: 135: 133: 129: 126: 121: 117: 113: 108: 104: 101: 97: 93: 90: 86: 82: 79: 77:Occupation(s) 75: 71: 61: 57: 53: 47: 43: 39: 34: 30: 22: 19: 1486:. 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Bill 193:machinist 115:Education 1488:June 30, 1465:12487984 1335:July 11, 1310:12487983 1263:June 30, 1258:ProQuest 1240:25701399 1096:June 30, 1068:June 30, 1019:, Sweden 948:13343781 653:36875587 492:12829469 372:Cal Tech 336:Kauzmann 183:Fellow. 1031:, Italy 841:4159793 833:1250371 805:Bibcode 645:3567326 602:5160255 594:3689874 551:4324047 543:2046766 515:Bibcode 483:1303070 454:Bibcode 356:α-helix 352:peptide 344:H-bonds 327:Kendrew 319:Pauling 308:β-sheet 304:α-helix 290:, with 167:at the 1463:  1455:  1415:  1308:  1300:  1238:  1230:  1218:: 51. 1092:. 1930 1064:. 1923 946:  917:  882:  874:  839:  831:  823:  797:Nature 782:671540 780:  772:  739:671540 737:  729:  694:  686:  651:  643:  635:  600:  592:  584:  549:  541:  533:  507:Nature 490:  480:  472:  276:assays 253:Career 132:Thesis 1149:(PDF) 1002:acids 995:1983 880:S2CID 837:S2CID 692:S2CID 649:S2CID 598:S2CID 547:S2CID 323:Corey 175:, a 1490:2022 1461:PMID 1453:ISSN 1413:ISSN 1337:2022 1306:PMID 1298:ISSN 1265:2022 1236:PMID 1228:ISSN 1098:2022 1070:2022 944:PMID 915:ISSN 872:ISSN 829:PMID 821:ISSN 778:PMID 770:ISSN 735:PMID 727:ISSN 684:ISSN 641:PMID 633:ISSN 590:PMID 582:ISSN 539:PMID 531:ISSN 488:PMID 470:ISSN 348:urea 321:and 306:and 94:and 59:Died 45:Born 1445:doi 1405:doi 1371:doi 1290:doi 1220:doi 1216:199 1171:doi 969:NIH 907:doi 864:doi 813:doi 801:259 762:doi 758:121 719:doi 715:121 676:doi 625:doi 574:doi 523:doi 511:351 478:PMC 462:doi 403:DNA 363:". 286:in 278:of 268:NIH 98:of 1506:: 1481:. 1459:. 1451:. 1439:. 1425:^ 1411:. 1399:. 1383:^ 1365:. 1328:. 1304:. 1296:. 1284:. 1256:. 1234:. 1226:. 1214:. 1210:. 1165:. 1106:^ 1088:. 1060:. 981:, 940:30 938:. 934:. 913:. 903:75 901:. 897:. 878:. 870:. 860:14 858:. 854:. 835:. 827:. 819:. 811:. 799:. 795:. 776:. 768:. 756:. 752:. 733:. 725:. 713:. 709:. 690:. 682:. 672:17 670:. 666:. 647:. 639:. 631:. 621:26 619:. 615:. 596:. 588:. 580:. 570:26 568:. 564:. 545:. 537:. 529:. 521:. 509:. 505:. 486:. 476:. 468:. 460:. 450:85 448:. 444:. 334:: 249:. 233:, 1492:. 1467:. 1447:: 1419:. 1407:: 1373:: 1339:. 1312:. 1292:: 1267:. 1222:: 1173:: 1151:. 1100:. 1072:. 1004:. 932:" 921:. 909:: 886:. 866:: 843:. 815:: 807:: 784:. 764:: 741:. 721:: 698:. 678:: 655:. 627:: 604:. 576:: 553:. 525:: 517:: 494:. 464:: 456::

Index


Philadelphia
Eugene, Oregon
Biophysical chemist
Thermodynamics
optical spectroscopies
biological macromolecules
Temple University
Princeton University
Thesis
The Theory of the Dielectric Properties of Ice
Walter Kauzmann
biophysical chemist
University of Oregon
National Academy of Sciences
Biophysical Society
American Physical Society
machinist
Great Depression
Irish ballads
Philadelphia Gas Works
Temple University
World War II
Walter Reed Hospital
G.I. Bill
Temple University
Phi Beta Kappa
Princeton University
Walter Kauzmann
U.S. Public Health Service

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