James K. Kranz, José C. Clemente (auth.), Aron W. Fenton's Allostery: Methods and Protocols PDF

By James K. Kranz, José C. Clemente (auth.), Aron W. Fenton (eds.)

ISBN-10: 1617793337

ISBN-13: 9781617793332

ISBN-10: 1617793345

ISBN-13: 9781617793349

Despite massive variability in the clinical group, allosteric rules can most sensible be outlined functionally as how a macromolecule binds one ligand another way while a moment ligand is or isn't really pre-bound to the macromolecule, which constitutes a necessary element of protein structure/function. In Allostery: equipment and Protocols, specialist researchers within the box supply key innovations to enquire this organic phenomenon. concentrating on heterotropic structures with a few insurance of homotropic structures, this quantity covers the tracking of allosteric functionality, allosteric conformational alterations, and allosteric alterations in protein dynamics/sub-population distribution, in addition to subject matters akin to macromolecular and ligand engineering of allosteric services and computational aids within the learn of allostery. Written within the hugely winning Methods in Molecular Biology™ sequence structure, the chapters comprise the type of particular description and implementation suggestion that's the most important for purchasing optimum ends up in the laboratory.

Thorough and intuitive, Allostery: equipment and Protocols aids scientists in carrying on with to review ligand-induced, through-protein results on protein functionality (ligand binding/catalysis), a phenomenon that's good well-known during the heritage of the lifestyles sciences and intensely poorly understood on the molecular level.

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K. (1996) Heterotropic effects of chloride on the ligation microstates of hemoglobin at constant water activity, Biophys. J. 71, 2106–2116. 15. Turner, G. , Doyle, M. , Pettigrew, D. , Turner, B. , Smith, F. , Rucknagel, D. , and Ackers, G. K. (1992) Mutagenic dissection of hemoglobin cooperativity: effects of amino acid alteration on subunit assembly of oxy and deoxy tetramers, Proteins: Struct. Funct. Genet. 14, 333–350. 16. Ip, S. H. , Johnson, M. , and Ackers, G. K. (1976) Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding: estimation of the equilibrium constant from forward and reverse rates, Biochemistry 15, 654–660.

USA 82, 5347–5351. 4. Ackers, G. , and Holt, J. M. (2006) Asymmetric cooperativity in a symmetric tetramer: Human hemoglobin, J. Biol. Chem. 281, 11441–11443. 5. Ackers, G. , Dalessio, P. , Lew, G. , Daugherty, M. , and Holt, J. M. (2002) Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer function, Proc. Natl. Acad. Sci. USA 99, 9777–9782. 6. , Doyle, M. , and Ackers, G. K. (1996) The oxygen-binding intermediates of human hemoglobin: evaluation of their contributions to cooperativity using zinc-containing hybrids, Biophys.

And Yarian, C. S. (2004) Analyzing intermediate state cooperativity in hemoglobin, In Methods in Enzymology (Holt, J. ), pp 3–28, Elsevier, San Diego, CA. 10. Holt, J. , Klinger, A. , Yarian, C. , and Ackers, G. K. (2005) Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 1. Cooperative and noncooperative oxygen binding in Zn-substituted hemoglobin, Biochemistry 44, 11925–11938. 11. Chu, A. , Turner, B. , and Ackers, G. K. (1984) Effects of protons on the oxygenationlinked subunit assembly in human hemoglobin, Biochemistry 23, 604–617.

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Allostery: Methods and Protocols by James K. Kranz, José C. Clemente (auth.), Aron W. Fenton (eds.)


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