MARC Record from marc_columbia

LEADER: 03471cam a2200373Ia 4500
001 4346709
005 20221102201022.0
008 040312t20042004caua b 001 0 eng d
035 $a(OCoLC)ocm54685204
035 $a(NNC)4346709
035 $a4346709
040 $aWJ7$cWJ7
245 00 $aEnergetics of biological macromolecules.$nPart E /$cedited by Jo M. Holt, Michael L. Johnson, Gary K. Ackers.
260 $aSan Diego :$bElsevier/Academic Press,$c[2004], ©2004.
300 $axxxiv, 443 pages, 4 unnumbered pages of plates :$billustrations (some color) ;$c24 cm.
336 $atext$btxt$2rdacontent
337 $aunmediated$bn$2rdamedia
490 1 $aMethods in enzymology,$x0076-6879 ;$vv. 380
504 $aIncludes bibliographical references and indexes.
505 0 $a1. Contributions to the catalytic efficiency of enzymes, and the binding of ligands to receptors, from improvements in packing within enzymes and receptors -- 2. Structural interpretation of pH and salt-dependent processes in proteins with computational methods -- 3. Electrostatic basis for bioenergetics -- 4. Local and global control mechanisms in allosteric threonine deaminase -- 5. Methods for analyzing cooperativity in phosphoglycerate dehydrogenase -- 6. Fluorescent probes applied to catalytic cooperativity in ATP synthase -- 7. Measurement of energetics of conformational change in cobalamin-dependent methionine synthase -- 8. Spectroscopic and kinetic methods for ligand-protein interactions of glutamate receptor -- 9. Quantitative analysis and interpretation of allosteric behavior -- 10. The immobilized template assay for measuring cooperativity in eukaryotic transcription complex assembly -- 11. Characterization of the cargo attachment complex of cytoplasmic dynein using NMR and mass spectrometry -- 12. Circular dichroism of protein-folding intermediates -- 13. Amide hydrogen exchange/mass spectrometry applied to cooperative protein folding: equilibrium unfolding of staphylococcus aureus aldolase -- 14. Kinetic and spectroscopic analysis of early events in protein folding -- 15. Hydrogen-exchange strategies applied to energetics of intermediate processes in protein folding -- 16. Cooperativity principles in protein folding -- 17. Native state hydrogen-exchange analysis of protein folding and protein motional domains -- 18. The preparations of F-labeled proteins for NMR studies.
650 0 $aMacromolecules.$0http://id.loc.gov/authorities/subjects/sh85079449
650 0 $aBioenergetics.$0http://id.loc.gov/authorities/subjects/sh85014133
650 0 $aAllosteric enzymes.$0http://id.loc.gov/authorities/subjects/sh85003711
650 0 $aProtein folding.$0http://id.loc.gov/authorities/subjects/sh89006334
650 0 $aThermodynamics.$0http://id.loc.gov/authorities/subjects/sh85134783
650 2 $aEnergy Metabolism.$0https://id.nlm.nih.gov/mesh/D004734
650 2 $aMacromolecular Substances.$0https://id.nlm.nih.gov/mesh/D046911
650 2 $aProtein Folding.$0https://id.nlm.nih.gov/mesh/D017510
650 2 $aThermodynamics.$0https://id.nlm.nih.gov/mesh/D013816
700 1 $aHolt, Jo M.$0http://id.loc.gov/authorities/names/no2004053055
700 1 $aJohnson, Michael L.,$d1947-$0http://id.loc.gov/authorities/names/nr92020805
700 1 $aAckers, Gary K.$0http://id.loc.gov/authorities/names/nr95036853
830 0 $aMethods in enzymology ;$vv. 380.$0http://id.loc.gov/authorities/names/n42016419
852 00 $boff,bio$hQP601$i.C71 v.380