- 题名/责任者:
- Energetics of biological macromolecules. Part D / edited by Jo M. Holt, Michael L. Johnson, Gary K. Ackers.
- 出版发行项:
- Amsterdam : Elsevier Academic Press, c2004.
- ISBN:
- 0121827836 (alk. paper) :
- 载体形态项:
- xxxii, 281 p., [4] p. of plates : ill. (some col.) ; 24 cm.
- 丛编题名:
- Methods in enzymology, 0076-6879 ; v. 379
- 附加个人名称:
- Ackers, Gary K.
- 附加个人名称:
- Holt, Jo M.
- 附加个人名称:
- Johnson, Michael L., 1947-
- 论题主题:
- Allosteric proteins.
- 论题主题:
- Thermodynamics.
- 论题主题:
- Macromolecules.
- 论题主题:
- Bioenergetics.
- 中图法分类号:
- Q55-5
- 书目附注:
- Includes bibliographical references and indexes.
- 内容附注:
- 1. Analyzing intermediate state cooperativity in hemoglobin -- 2. Nuclear magnetic resonance spectroscopy in the study of hemoglobin cooperativity -- 3. Evaluating cooperativity in dimeric hemoglobins -- 4. Measuring assembly and binding in human embryonic hemoglobins -- 5. Small-angle scattering techniques for analyzing conformational transitions in hemocyanins -- 6. Multivalent protein-carbohydrate interactions: isothermal titration microcalorimetry studies -- 7. Calorimetric analysis of mutagenic effects on protein-ligand interactions -- 8. Multiple binding of ligands to a linear biopolymer -- 9. Probing site-specific energetics in proteins and nucleic acids by hydrogen exchange and nuclear magnetic resonance spectroscopy -- 10. Fluorescence quenching methods to study protein-nucleic acid interactions -- 11. Thermodynamics, protein modification, and molecular dynamics in characterizing lactose repressor protein: strategies for complex analyses of protein structure-function -- 12. Linked equilibria in biotin repressor function: thermodynamic, structural and kinetic analysis -- 13. Distance parameters derived from time-resolved Forster resonance energy transfer measurements and their use in structural interpretations of thermodynamic quantities associated with protein-DNA interactions.
- 随书光盘:
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