| Title | TI-205 nuclear magnetic resonance determination of the thermodynamic parameters for the binding of monovalent cations to gramicidins A and C. |
| Publication Type | Journal Article |
| Year of Publication | 1988 |
| Authors | Hinton JF, Fernandez JQ, Shungu DC, Whaley WL, Koeppe RE, Millett FS |
| Journal | Biophys J |
| Volume | 54 |
| Issue | 3 |
| Pagination | 527-33 |
| Date Published | 1988 Sep |
| ISSN | 0006-3495 |
| Keywords | Gramicidin, Ion Channels, Magnetic Resonance Spectroscopy, Models, Biological, Models, Molecular, Protein Binding, Protein Conformation, Thallium, Thermodynamics |
| Abstract | Thermodynamic parameters for the binding of the monovalent cations, Li+, Na+, K+, Rb+, Cs+, NH4+, TI+, and Ag+, to gramicidin A and for the binding of TI+ to gramicidin C, incorporated into lysophosphatidylcholine, have been determined using a combination of TI-205 nuclear magnetic resonance spectroscopy and competition binding. The thermodynamic parameters, enthalpy and entropy, are discussed in terms of a process involving the transfer of cations from an aqueous to amide environment. |
| DOI | 10.1016/S0006-3495(88)82985-0 |
| Alternate Journal | Biophys J |
| PubMed ID | 2462930 |
| PubMed Central ID | PMC1330351 |
| Grant List | GM-34968 / GM / NIGMS NIH HHS / United States RR07101 / RR / NCRR NIH HHS / United States |
Related Institute:
MRI Research Institute (MRIRI)