シクロール仮説とは? わかりやすく解説

Weblio 辞書 > 辞書・百科事典 > 百科事典 > シクロール仮説の意味・解説 

シクロール仮説

出典: フリー百科事典『ウィキペディア(Wikipedia)』 (2022/11/05 20:39 UTC 版)

シクロール仮説(シクロールかせつ、: cyclol hypothesis)は、折り畳まれた球状タンパク質の初の構造モデルである[1]。1930年代末にドロシー・リンチによって構築された本仮説は3つの仮定に基づいている。まずはじめに、本仮説は、2つのペプチド結合シクロール反応(図1)によって架橋されうることを仮定する。これらの架橋はペプチド基間の「非共有結合性」水素結合共有結合版である。これらの反応はエルゴペプチド類やその他の化合物において観察される。次に、ある条件下において、アミノ酸が自然に可能な最大の数のシクロール架橋を作り、シクロール分子(図2)およびシクロール生地(cyclol fabrics; 図3)が生じることを仮定する。これらのシクロール分子およびシクロール生地はこれまで観察されたことはない。最後に、本仮説は、球状タンパク質が自由端を持たないシクロール生地から形成されるプラトン立体および半正多面体に対応する三次構造を持つことを仮定する。こういった「閉シクロール」分子についても観察されたことはない。


  1. ^ Tiselius, A (1939). “The Chemistry of Proteins and Amino Acids”. Annual Review of Biochemistry 8: 155–184. doi:10.1146/annurev.bi.08.070139.001103. 
  2. ^ a b Svedberg, T (1929). “Mass and size of protein molecules”. Nature 123 (3110): 871. Bibcode1929Natur.123..871S. doi:10.1038/123871a0. 
  3. ^ a b Svedberg, T (1934). “Sedimentation of molecules in centrifugal fields”. Chemical Reviews 14: 1–15. doi:10.1021/cr60047a001. 
  4. ^ a b c Bergmann, M; Niemann C (1937). “On the structure of proteins: cattle hemoglobin, egg albumin, cattle fibrin, and gelatin”. Journal of Biological Chemistry 118: 301–314. doi:10.1016/S0021-9258(18)74540-7. 
  5. ^ Svedberg, T (1930). “The pH Stability Regions of Proteins”. Transactions of the Faraday Society 26: 741–744. doi:10.1039/TF9302600737. 
  6. ^ Fruton, JS (1979). “Early theories of protein structure”. Annals of the New York Academy of Sciences 325 (1): 1–18. Bibcode1979NYASA.325....1F. doi:10.1111/j.1749-6632.1979.tb14125.x. PMID 378063. 
  7. ^ Hofmeister, F (1902). “Über Bau und Gruppierung der Eiweisskörper”. Ergebnisse der Physiologie 1: 759–802. doi:10.1007/BF02323641. 
  8. ^ Fischer, E (1902). “Über die Hydrolyse der Proteinstoffe”. Chemiker Zeitung 26: 939–940. 
  9. ^ Fischer, E (1913). “Synthese von Depsiden, Flechtenstoffen und Gerbstoffen”. Berichte der Deutschen Chemischen Gesellschaft 46 (3): 3253–3289. doi:10.1002/cber.191304603109. https://zenodo.org/record/1426525. 
  10. ^ Sørensen, SPL (1930). “The constitution of soluble proteins as reversibly dissociable component systems”. Comptes Rendus des Travaux du Laboratoire Carlsberg 18: 1–124. 
  11. ^ Fruton, JS (1999). Proteins, Enzymes, Genes: The Interplay of Chemistry and Biology. New Haven, CT: Yale University Press. ISBN 0-585-35980-6 
  12. ^ Abderhalden, E (1924). “Diketopiperazines”. Naturwissenschaften 12 (36): 716–720. Bibcode1924NW.....12..716A. doi:10.1007/BF01504819. 
  13. ^ Abderhalden, E; Komm E (1924). “Über die Anhydridstruktur der Proteine”. Zeitschrift für Physiologische Chemie 139 (3–4): 181–204. doi:10.1515/bchm2.1924.139.3-4.181. 
  14. ^ Linderstrøm-Lang, K; Hotchkiss RD; Johansen G (1938). “Peptide Bonds in Globular Proteins”. Nature 142 (3605): 996. Bibcode1938Natur.142..996L. doi:10.1038/142996a0. 
  15. ^ Chick, H; Martin CJ (1910). “On the "Heat" Coagulation of Proteins”. Journal of Physiology 40 (5): 404–430. doi:10.1113/jphysiol.1910.sp001378. PMC 1533708. PMID 16993016. https://zenodo.org/record/1433580. 
  16. ^ Chick, H; Martin CJ (1911). “On the "Heat" Coagulation of Proteins. II. The Action of Hot Water upon Egg-albumen and the Influence of Acid and Salts upon Reaction Velocity”. Journal of Physiology 43 (1): 1–27. doi:10.1113/jphysiol.1911.sp001456. PMC 1512746. PMID 16993081. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1512746/. 
  17. ^ Chick, H; Martin CJ (1912). “On the "Heat" Coagulation of Proteins. III. The Influence of Alkali upon Reaction Velocity”. Journal of Physiology 45 (1–2): 61–69. doi:10.1113/jphysiol.1912.sp001535. PMC 1512881. PMID 16993182. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1512881/. 
  18. ^ Chick, H; Martin CJ (1912). “On the "Heat" Coagulation of Proteins. IV. The Conditions controlling the Agglutination of Proteins already acted upon by Hot Water”. Journal of Physiology 45 (4): 261–295. doi:10.1113/jphysiol.1912.sp001551. PMC 1512885. PMID 16993156. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1512885/. 
  19. ^ Anson, ML; Mirsky AE (1929). “Protein Coagulation and Its Reversal”. Journal of General Physiology 13 (2): 121–132. doi:10.1085/jgp.13.2.121. PMC 2141032. PMID 19872511. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141032/. 
  20. ^ a b Anson, ML (1945). “Protein Denaturation and the Properties of Protein Groups”. Advances in Protein Chemistry 2: 361–386. doi:10.1016/S0065-3233(08)60629-4. ISBN 978-0-12-034202-0. 
  21. ^ Wu, H (1931). “Studies on Denaturation of Proteins. XIII. A Theory of Denaturation”. Chinese Journal of Physiology 5: 321–344.  Preliminary reports were presented before the XIIIth International Congress of Physiology at Boston (19–24 August 1929) and in the October 1929 issue of the American Journal of Physiology.
  22. ^ a b Mirsky, AE; Pauling L (1936). “On the Structure of Native, Denatured, and Coagulated Proteins”. Proceedings of the National Academy of Sciences of the United States of America 22 (7): 439–447. Bibcode1936PNAS...22..439M. doi:10.1073/pnas.22.7.439. PMC 1076802. PMID 16577722. http://authors.library.caltech.edu/4485/1/MIRpnas36.pdf. 
  23. ^ Neurath, H; Greenstein JP; Putnam FW; Erickson JO (1944). “The Chemistry of Protein Denaturation”. Chemical Reviews 34 (2): 157–265. doi:10.1021/cr60108a003. 
  24. ^ Putnam, F (1953). “Protein Denaturation”. The Proteins (H. Neurath and K. Bailey, Eds.) 1B: 807–892. 
  25. ^ Astbury, WT; Woods HJ (1931). “The Molecular Weight of Proteins”. Nature 127 (3209): 663–665. Bibcode1931Natur.127..663A. doi:10.1038/127663b0. 
  26. ^ Astbury, WT (1933). “Some Problems in the X-Ray Analysis of the Structure of Animal Hairs and Other Protein Fibres”. Transactions of the Faraday Society 29 (140): 193–211. doi:10.1039/tf9332900193. 
  27. ^ a b Jordan Lloyd, D (1932). “Colloidal Structure and its Biological Significance”. Biological Reviews 7 (3): 254–273. doi:10.1111/j.1469-185x.1962.tb01043.x. 
  28. ^ Jordan Lloyd, D; Marriott (1933). “Title unknown”. Transactions of the Faraday Society 29: 1228. doi:10.1039/tf9332901228. 
  29. ^ Astbury, WT (1936). “Unknown title”. Journal of the Textile Institute 27: 282–?. 
  30. ^ Wrinch, DM (1936). “The Pattern of Proteins”. Nature 137 (3462): 411–412. Bibcode1936Natur.137..411W. doi:10.1038/137411a0. 
  31. ^ Wrinch, DM (1936). “Energy of Formation of 'Cyclol' Molecules”. Nature 138 (3484): 241–242. Bibcode1936Natur.138..241W. doi:10.1038/138241a0. 
  32. ^ Frank, FC (1936). “Energy of Formation of 'Cyclol' Molecules”. Nature 138 (3484): 242. Bibcode1936Natur.138..242F. doi:10.1038/138242a0. 
  33. ^ Langmuir, I; Wrinch DM (1939). “Nature of the Cyclol Bond”. Nature 143 (3611): 49–52. Bibcode1939Natur.143...49L. doi:10.1038/143049a0. 
  34. ^ Langmuir, I (1939). “The Structure of Proteins”. Proceedings of the Physical Society 51 (4): 592–612. Bibcode1939PPS....51..592L. doi:10.1088/0959-5309/51/4/305. 
  35. ^ Wrinch, DM (1938). “On the Hydration and Denaturation of Proteins”. Philosophical Magazine 25: 705–739. 
  36. ^ Wrinch, DM (1936). “Hydration and Denaturation of Proteins”. Nature 142 (3588): 260. Bibcode1938Natur.142..259.. doi:10.1038/142259a0. 
  37. ^ Dow, RB; Matthews JE; Jr. and Thorp WTS (1940). “The Effect of High Pressure Treatment on the Physiological Activity of Insulin”. American Journal of Physiology 131 (2): 382–387. doi:10.1152/ajplegacy.1940.131.2.382. 
  38. ^ Kauzmann, W (1959). “Some Factors in the Interpretation of Protein Denaturation”. Advances in Protein Chemistry 14: 1–63. doi:10.1016/S0065-3233(08)60608-7. ISBN 978-0-12-034214-3. PMID 14404936. 
  39. ^ Wrinch, DM (1936). “Structure of Proteins and of Certain Physiologically Active Compounds”. Nature 138 (3493): 651–652. Bibcode1936Natur.138..651W. doi:10.1038/138651a0. 
  40. ^ Wrinch, DM; Jordan Lloyd D (1936). “The Hydrogen Bond and the Structure of Proteins”. Nature 138 (3496): 758–759. Bibcode1936Natur.138..758W. doi:10.1038/138758a0. 
  41. ^ Wrinch, DM (1937). “Nature of the Linkage in Proteins”. Nature 139 (3521): 718. Bibcode1937Natur.139..718W. doi:10.1038/139718a0. 
  42. ^ Astbury, WT; Wrinch DM (1937). “Intramolecular Folding of Proteins by Keto-Enol Interchange”. Nature 139 (3523): 798. Bibcode1937Natur.139..798A. doi:10.1038/139798a0. 
  43. ^ Wrinch, D. “The Fabric Theory of Protein Structure”. Philosophical Magazine 30: 64–67. 
  44. ^ Wrinch, DM (1937). “The Cyclol Theory and the 'Globular' Proteins”. Nature 139 (3527): 972–973. Bibcode1937Natur.139..972W. doi:10.1038/139972a0. 
  45. ^ Wrinch, DM (1947). “The Native Protein”. Science 106 (2743): 73–76. Bibcode1947Sci...106...73W. doi:10.1126/science.106.2743.73. PMID 17808858. 
  46. ^ Wrinch, DM (1937). “On the Pattern of Proteins”. Proceedings of the Royal Society A160: 59–86. 
    Wrinch, DM (1937). “The Cyclol Hypothesis and the "Globular" Proteins”. Proceedings of the Royal Society A161: 505–524. 
    Wrinch, DM (1938). “On the Molecular Weights of the Globular Proteins”. Philosophical Magazine 26: 313–332. 
  47. ^ Wrinch, DM (1939). “The Tuberculin Protein TBU-Bovine (523)”. Nature 144 (3636): 77. Bibcode1939Natur.144...77W. doi:10.1038/144077a0. 
  48. ^ Wrinch, DM (1937). “On the structure of pepsin”. Philosophical Magazine 24: 940. 
  49. ^ Wrinch, DM (1938). “Structure of Pepsin”. Nature 142 (3587): 217. Bibcode1938Natur.142..215.. doi:10.1038/142215a0. 
  50. ^ Wrinch, DM (1937). “On the Structure of Insulin”. Science 85 (2215): 566–567. Bibcode1937Sci....85..566W. doi:10.1126/science.85.2215.566. PMID 17769864. 
  51. ^ Wrinch, DM (1937). “On the Structure of Insulin”. Transactions of the Faraday Society 33: 1368–1380. doi:10.1039/tf9373301368. 
  52. ^ Wrinch, DM (1938). “The Structure of the Insulin Molecule”. Journal of the American Chemical Society 60 (8): 2005–2006. doi:10.1021/ja01275a514. 
  53. ^ Wrinch, DM (1938). “The Structure of the Insulin Molecule”. Science 88 (2276): 148–149. Bibcode1938Sci....88..148W. doi:10.1126/science.88.2276.148-a. PMID 17751525. 
  54. ^ Wrinch, DM; Langmuir I (1938). “The Structure of the Insulin Molecule”. Journal of the American Chemical Society 60 (9): 2247–2255. doi:10.1021/ja01276a062. 
  55. ^ Langmuir, I; Wrinch DM (1939). “A Note on the Structure of Insulin”. Proceedings of the Physical Society 51 (4): 613–624. Bibcode1939PPS....51..613L. doi:10.1088/0959-5309/51/4/306. 
  56. ^ Bragg, WL (1939). “Patterson Diagrams in Crystal Analysis”. Nature 143 (3611): 73–74. Bibcode1939Natur.143...73B. doi:10.1038/143073a0. 
  57. ^ Bernal, JD (1939). “Vector Maps and the Cyclol Hypothesis”. Nature 143 (3611): 74–75. Bibcode1939Natur.143...74B. doi:10.1038/143074a0. 
  58. ^ Robertson, JM (1939). “Vector Maps and Heavy Atoms in Crystal Analysis and the Insulin Structure”. Nature 143 (3611): 75–76. Bibcode1939Natur.143...75R. doi:10.1038/143075a0. 
  59. ^ Riley, DP; Fankuchen I (1939). “A Derived Patterson Analysis of the Skeleton of the Cyclol C2 Molecule”. Nature 143 (3624): 648–649. Bibcode1939Natur.143..648R. doi:10.1038/143648a0. 
  60. ^ Wrinch, DM (1940). “Patterson Projection of the Skeletons of the Structure proposed for the Insulin Molecule”. Nature 145 (3687): 1018. Bibcode1940Natur.145.1018W. doi:10.1038/1451018a0. 
  61. ^ Riley, D (1940). “A Patterson Analysis derived from the Cyclol C2 Skeleton”. Nature 146 (3694): 231. Bibcode1940Natur.146..231R. doi:10.1038/146231a0. 
  62. ^ Neurath, H; Bull HB (1938). “The Surface Activity of Proteins”. Chemical Reviews 23 (3): 391–435. doi:10.1021/cr60076a001. 
  63. ^ Huggins, M (1939). “The Structure of Proteins”. Journal of the American Chemical Society 61 (3): 755. doi:10.1021/ja01872a512. 
  64. ^ Haurowitz, F (1938). “Die Anordnung der Peptidketten in Sphäroprotein-Molekülen”. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 256: 28–32. doi:10.1515/bchm2.1938.256.1.28. 
  65. ^ Meyer, KH; Hohenemser W (1938). “Possibility of the Formation of Cyclols from Simple Peptides”. Nature 141 (3582): 1138–1139. Bibcode1938Natur.141.1138M. doi:10.1038/1411138b0. 
  66. ^ Bergmann, M; Niemann C (1938). “The Chemistry of Amino Acids and Proteins”. Annual Review of Biochemistry 7 (2): 99–124. doi:10.1146/annurev.bi.07.070138.000531. PMC 537431. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC537431/. 
  67. ^ Neuberger, A (1939). “Chemical criticism of the cyclol and frequency hypothesis of protein structure”. Proceedings of the Royal Society 170: 64–65. 
  68. ^ Neuberger, A (1939). “Chemical Aspects of the Cyclol Hypothesis”. Nature 143 (3620): 473. Bibcode1939Natur.143..473N. doi:10.1038/143473a0. 
  69. ^ Haurowitz, F; Astrup T (1939). “Ultraviolet absorption of genuine and hydrolysed protein”. Nature 143 (3612): 118–119. Bibcode1939Natur.143..118H. doi:10.1038/143118b0. 
  70. ^ Klotz, IM; Griswold P (1949). “Infrared Spectra and the Amide Linkage in a Native Globular Protein”. Science 109 (2830): 309–310. Bibcode1949Sci...109..309K. doi:10.1126/science.109.2830.309. PMID 17782718. 
  71. ^ a b Pauling, L; Niemann C (1939). “The Structure of Proteins”. Journal of the American Chemical Society 61 (7): 1860–1867. doi:10.1021/ja01876a065. 
  72. ^ Hotchkiss, RD (1939). “The Determination of Peptide Bonds in Crystalline Lactoglobulin”. Journal of Biological Chemistry 131: 387–395. doi:10.1016/S0021-9258(18)73511-4. 
  73. ^ Wrinch, DM (1941). “The Geometrical Attack on Protein Structure”. Journal of the American Chemical Society 63 (2): 330–33. doi:10.1021/ja01847a004. 
  74. ^ Wrinch, DM (1940). “The Cyclol Hypothesis”. Nature 145 (3678): 669–670. Bibcode1940Natur.145..669W. doi:10.1038/145669a0. 
  75. ^ a b Wrinch, DM (1948). “The Native Proteins as Polycondensations of Amino Acids”. Science 107 (2783): 445–446. Bibcode1948Sci...107R.445W. doi:10.1126/science.107.2783.445-a. PMID 17844448. 
  76. ^ Wrinch, DM (1948). “Skeletal Units in Protein Crystals”. Science 115 (2987): 356–357. Bibcode1952Sci...115..356W. doi:10.1126/science.115.2987.356. PMID 17748855. 
  77. ^ Wrinch, DM (1948). “Molecules of the Insulin Structure”. Science 116 (3021): 562–564. Bibcode1952Sci...116..562W. doi:10.1126/science.116.3021.562. PMID 13015111. 
  78. ^ Wrinch, DM (1939). “The Structure of the Globular Proteins”. Nature 143 (3620): 482–483. Bibcode1939Natur.143..482W. doi:10.1038/143482a0. 
  79. ^ Wrinch, DM (1939). “The Cyclol Theory and the Structure of Insulin”. Nature 143 (3627): 763–764. Bibcode1939Natur.143..763W. doi:10.1038/143763a0. 
  80. ^ Wrinch, DM (1939). “Native Proteins, Flexible Frameworks and Cytoplasmic Organization”. Nature 150 (3800): 270–271. Bibcode1942Natur.150..270W. doi:10.1038/150270a0. 
  81. ^ Anslow, GA (1942). “Bond Energies in Some Protein Fabrics and Side Chains”. Physical Review 61 (7–8): 547. Bibcode1942PhRv...61..541.. doi:10.1103/PhysRev.61.541. 
  82. ^ Anslow, GA (1945). “Ultraviolet Spectra of Biologically Important Molecules”. Journal of Applied Physics 16 (1): 41–49. Bibcode1945JAP....16...41A. doi:10.1063/1.1707499. 
  83. ^ Anslow, GA (1953). “The Sites of the Amino-Acid Residues on a Cyclol Model of Insulin”. Journal of Chemical Physics 21 (11): 2083–2084. Bibcode1953JChPh..21.2083A. doi:10.1063/1.1698765. 
  84. ^ Guedez, T; Núñez A; Tineo E; Núñez O (2002). “Ring size configuration effect and the transannular intrinsic rates in bislactam macrocycles”. Journal of the Chemical Society, Perkin Transactions 2 2002 (12): 2078–2082. doi:10.1039/b207233e. 
  85. ^ Bernal, JD (1939). “Structure of proteins”. Nature 143 (3625): 663–667. Bibcode1939Natur.143..663B. doi:10.1038/143663a0. 
  86. ^ Wieland T and Bodanszky M, The World of Peptides, Springer Verlag, pp.193–198. ISBN 0-387-52830-X
  87. ^ Hofmann, A; Ott H; Griot R; Stadler PA; Frey AJ (1963). “Synthese von Ergotamin”. Helvetica Chimica Acta 46: 2306–2336. doi:10.1002/hlca.19630460650. 
  88. ^ Shemyakin, MM; Antonov VK; Shkrob AM (1963). “Activation of the amide group by acylation”. Peptides, Proc. 6th Europ. Pept. Symp., Athens: 319–328. 
  89. ^ Zanotti, G; Pinnen F; Lucente G; Cerrini S; Fedeli W; Mazza F (1984). “Peptide thiacyclols. Synthesis and structural studies”. J. Chem. Soc. Perkin Trans. 1: 1153–1157. doi:10.1039/p19840001153. 
  90. ^ Griot, RG; Frey AJ (1963). “The formation of cyclols from N-hydroxyacyl lactames”. Tetrahedron 19 (11): 1661–1673. doi:10.1016/S0040-4020(01)99239-7. 
  91. ^ Lucente, G; Romeo A (1971). “Synthesis of cyclols from small peptides via amide-amide reaction”. Chem. Commun. ?: 1605–1607. doi:10.1039/c29710001605. 
  92. ^ Rothe M, Schindler W, Pudill R, Kostrzewa U, Theyson R, and Steinberger R. (1971) "Zum Problem der Cycloltripeptidsynthese", Peptides, Proc. 11th Europ. Pept. Symp., Wien, 388–399.
  93. ^ Rothe M and Roser KL. (1988) "Conformational flexibility of cyclic tripeptides", Abstr. 20th Europ. Pept. Symp. Tübingen, p. 36.
  94. ^ Wieland T and Mohr H. (1956) "Diacylamide als energiereiche Verbindungen. Diglycylimid", Liebigs Ann. Chem., 599, 222–232.
  95. ^ Wieland T and Urbach H. (1958) "Weitere Di-Aminoacylimide und ihre intramolekulare Umlagerung", Liebigs Ann. Chem., 613, 84–95.
  96. ^ Brenner, M (1958). “The aminoacyl insertion”. Ciba Foundation Symposium on Amino Acids and Peptides with Antimetabolic Activity. 
  97. ^ Wrinch, DM (1957). “Structure of Bacitracin A”. Nature 179 (4558): 536–537. Bibcode1957Natur.179..536W. doi:10.1038/179536a0. 
  98. ^ Wrinch, DM (1957). “An Approach to the Synthesis of Polycyclic Peptides”. Nature 180 (4584): 502–503. Bibcode1957Natur.180..502W. doi:10.1038/180502b0. 
  99. ^ Wrinch, DM (1962). “Some Issues in Molecular Biology and Recent Advances in the Organic Chemistry of Small Peptides”. Nature 193 (4812): 245–247. Bibcode1962Natur.193..245W. doi:10.1038/193245a0. PMID 14008494. 
  100. ^ Wrinch, DM (1963). “Recent Advances in Cyclol Chemistry”. Nature 199 (4893): 564–566. Bibcode1963Natur.199..564W. doi:10.1038/199564a0. 
  101. ^ Wrinch, DM (1965). “A Contemporary Picture of the Chemical Aspects of Polypeptide Chain Structures and Certain Problems of Molecular Biology”. Nature 206 (4983): 459–461. Bibcode1965Natur.206..459W. doi:10.1038/206459a0. PMID 5319104. 
  102. ^ Wrinch, DM (1960). Chemical Aspects of the Structures of Small Peptides: An Introduction. Copenhagen: Munksgaard 
  103. ^ Wrinch, DM (1965). Chemical Aspects of Polypeptide Chain Structures and the Cyclol Theory. New York: Plenum Press 
  104. ^ Kauzmann, W (1993). “Reminiscences from a life in protein physical chemistry”. Protein Science 2 (4): 671–691. doi:10.1002/pro.5560020418. PMC 2142355. PMID 8518739. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142355/. 
  105. ^ Tanford, C; Reynolds J (2001). Nature's robots: A history of proteins. Oxford: Oxford University Press. ISBN 0-19-850466-7. https://archive.org/details/naturesrobotshis0000tanf 
  106. ^ Pais, A (1986). Inward Bound: Of Matter and Forces in the Physical World. Oxford University Press. ISBN 0-19-851971-0. https://archive.org/details/inwardboundofmat00pais_0 
    Bohr, N (1913). “On the Constitution of Atoms and Molecules (Part 1 of 3)”. Philosophical Magazine 26: 1–25. Bibcode1913PMag...26....1B. doi:10.1080/14786441308634955. オリジナルの2007-07-04時点におけるアーカイブ。. https://web.archive.org/web/20070704225134/http://dbhs.wvusd.k12.ca.us/webdocs/Chem-History/Bohr/Bohr-1913a.html. 
  107. ^ Bohr, N (1913). “On the Constitution of Atoms and Molecules, Part II Systems Containing Only a Single Nucleus”. Philosophical Magazine 26 (153): 476–502. Bibcode1913PMag...26..476B. doi:10.1080/14786441308634993. https://zenodo.org/record/1430916. 
  108. ^ Bohr, N (1913). “On the Constitution of Atoms and Molecules, Part III”. Philosophical Magazine 26: 857–875. Bibcode1913PMag...26..857B. doi:10.1080/14786441308635031. https://zenodo.org/record/1430922. 
  109. ^ Bohr, N (1914). “The spectra of helium and hydrogen”. Nature 92 (2295): 231–232. Bibcode1913Natur..92..231B. doi:10.1038/092231d0. https://zenodo.org/record/1429570. 
  110. ^ Pauling, L; Corey RB (1953). “A Proposed Structure For The Nucleic Acids”. Proceedings of the National Academy of Sciences 39 (2): 84–97. Bibcode1953PNAS...39...84P. doi:10.1073/pnas.39.2.84. PMC 1063734. PMID 16578429. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1063734/. 
  111. ^ Franklin, RE; Gosling R (1953). “Molecular configuration of sodium thymonucleate”. Nature 171 (4356): 740–741. Bibcode1953Natur.171..740F. doi:10.1038/171740a0. PMID 13054694. 
  112. ^ a b Watson, JD; Crick F (1953). “Molecular structure of nucleic acids: A structure for deoxyribonucleic acid”. Nature 171 (4356): 737–738. Bibcode1953Natur.171..737W. doi:10.1038/171737a0. PMID 13054692. 
  113. ^ Saenger, W (1988). Principles of Nucleic Acid Structure. Springer Verlag. ISBN 0-387-90762-9 
  114. ^ Pais, A. (1982). Subtle is the Lord: The Science and the Life of Albert Einstein. Oxford University Press. ISBN 0-19-853907-X. https://archive.org/details/subtleislordscie00pais 





英和和英テキスト翻訳>> Weblio翻訳
英語⇒日本語日本語⇒英語
  
  •  シクロール仮説のページへのリンク

辞書ショートカット

すべての辞書の索引

「シクロール仮説」の関連用語

シクロール仮説のお隣キーワード
検索ランキング

   

英語⇒日本語
日本語⇒英語
   



シクロール仮説のページの著作権
Weblio 辞書 情報提供元は 参加元一覧 にて確認できます。

   
ウィキペディアウィキペディア
All text is available under the terms of the GNU Free Documentation License.
この記事は、ウィキペディアのシクロール仮説 (改訂履歴)の記事を複製、再配布したものにあたり、GNU Free Documentation Licenseというライセンスの下で提供されています。 Weblio辞書に掲載されているウィキペディアの記事も、全てGNU Free Documentation Licenseの元に提供されております。

©2024 GRAS Group, Inc.RSS