Zobrazeno 1 - 10
of 97
pro vyhledávání: '"John A. Schellman"'
Autor:
John A. Schellman
Publikováno v:
Protein Science. 19:363-371
Walter Kauzmann came to Princeton in 1946 to replace his former mentor, Henry Eyring, who went back to Salt Lake City and his Mormon roots. He has written about his reminiscences in physical chemistry, proteins, and related topics in Protein Science,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80237e98953d2ae51aeb7223b03c3dce
https://doi.org/10.1002/pro.328
https://doi.org/10.1002/pro.328
Autor:
John A. Schellman
Publikováno v:
Quarterly Reviews of Biophysics. 38:351-361
Introduction 351Part I. A succession of concepts 3521. Cooperativity 3522. Cosolvent interaction 3523. Linearity 3544. Solvent exchange 3545. Excluded volume 3566. Summation 357Part II 1. The Kirkwood–Buff approach 357Acknowledgments 360References
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ba8d3a459eeb14fbf569867b8ad8077
https://doi.org/10.1017/s0033583505004099
https://doi.org/10.1017/s0033583505004099
Autor:
John A. Schellman
Publikováno v:
Biophysical Chemistry. 105:161-165
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::736b345af7c39df1d2496d2e11d5b09b
https://doi.org/10.1016/s0301-4622(03)00078-4
https://doi.org/10.1016/s0301-4622(03)00078-4
Autor:
Rainer Jaenicke, John A. Schellman
Publikováno v:
Biophysical Chemistry. 100:1-7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f71b2880ff4fcd98fba84cc57d2553a7
https://doi.org/10.1016/s0301-4622(02)00257-0
https://doi.org/10.1016/s0301-4622(02)00257-0
Autor:
John A. Schellman, Hong Qian
Publikováno v:
The Journal of Physical Chemistry B. 104:11528-11540
For many applications, charge distributions around macromolecules in aqueous solution are of greater interest than the electrical potential. We show that it is possible to use the Poisson−Boltzmann...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ac500a2cd71c77d11ed1cafa78d6f38c
https://doi.org/10.1021/jp994168m
https://doi.org/10.1021/jp994168m
Autor:
John A. Schellman, Howard R. Reese
Publikováno v:
Biopolymers. 39:161-171
Though the nearest neighbor exclusion model provides a good semiquantitative description of intercalation isotherms, it ignores the electrostatic interaction between cationic intercalators and DNA and underestimates binding in the neighborhood of θ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5d54daec278ed614680d1b3b5bddb02c
https://doi.org/10.1002/(sici)1097-0282(199608)39:2<161::aid-bip4>3.0.co
https://doi.org/10.1002/(sici)1097-0282(199608)39:2<161::aid-bip4>3.0.co
Publikováno v:
Protein Science. 6:1092-1100
The Carlsberg Laboratory in Copenhagen has had a long tradition of outstanding science. At the time covered by this discussion, Kjeldahl, Sørensen, and Linderstrøm-Lang had been consecutive directors of the Chemical Laboratory for 83 years. Lang's
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc6bd2db2fa679bf5ddde75a7e652b59
https://doi.org/10.1002/pro.5560060516
https://doi.org/10.1002/pro.5560060516
Autor:
John A. Schellman
Publikováno v:
Biophysical Chemistry. 64:7-13
Molecular concepts have been gradually incorporated into chemical thermodynamics. This is done by applying standard thermodynamics manipulations to systems which are restricted by the assumption of a specific molecular model or mechanism. Here we tra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e11b47d3cb0be30e70cd2acf2381557c
https://doi.org/10.1016/s0301-4622(96)02206-5
https://doi.org/10.1016/s0301-4622(96)02206-5
Autor:
George N. Somero, John A. Schellman
Publikováno v:
Biophysical Journal. 71(4):1985-1993
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bf5f595696f342354a9793378efdd9c
Autor:
Nadine C. Gassner, John A. Schellman
Publikováno v:
Biophysical Chemistry. 59:259-275
G. Makhatadze and P. Privalov [J. Mol. Biol., 226 (1995) 491] have recently measured the enthalpy of transfer of three proteins into urea and guanidinium chloride solutions as a function of concentration and temperature. The present paper applies the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef744d291917adb6d0d9e5d45d465142
https://doi.org/10.1016/0301-4622(95)00130-1
https://doi.org/10.1016/0301-4622(95)00130-1