MARC Record from marc_columbia

LEADER: 02896fam a2200409 a 4500
001 4050480
005 20221027024604.0
008 950330s1995 nyua b 000 0 eng
010 $a 95015257
020 $a0521416590 (hc)
035 $a(OCoLC)501483620
035 $a(OCoLC)ocn501483620
035 $9ALE5537HS
035 $a(NNC)4050480
035 $a4050480
040 $aDLC$cDLC$dNNC-M$dOrLoB-B
050 00 $aQP517.B42$bD5 1996
082 00 $a574.192$220
100 1 $aDi Cera, Enrico.$0http://id.loc.gov/authorities/names/n95031424
245 10 $aThermodynamic theory of site-specific binding processes in biological macromolecules /$cEnrico Di Cera.
260 $aNew York :$bCambridge University Press,$c1995.
300 $axvi, 296 pages :$billustrations ;$c26 cm
336 $atext$btxt$2rdacontent
337 $aunmediated$bn$2rdamedia
504 $aIncludes bibliographical references.
505 00 $g1.$tStatistical thermodynamic foundations --$g2.$tGlobal binding processes --$g3.$tLocal binding processes --$g4.$tSpecific cases and applications --$g5.$tSite-specific effects in Ising networks.
520 $aThis book provides the first systematic treatment of the thermodynamic theory of site-specific effects in biological macromolecules. It describes the phenomenological and conceptual bases required to allow a mechanistic understanding of these effects from analysis of experimental data.
520 8 $aThe thermodynamic theory also results in novel experimental strategies that enable the derivation of information on local, site-specific properties of a macromolecular system from analysis of perturbed global properties. The treatment focuses on binding phenomena, but is amenable to extension both conceptually and formally to the analysis of other cooperative processes, such as protein folding and helix-coil transitions.
520 8 $aMuch attention is devoted to the analysis of mutational perturbations used as probes of site-specific energetics. The arrangement of various sections in the book allows its use both as a reference work on cooperative binding phenomena for any scientist involved in structure-function studies of biological macromolecules, and as a text for graduate students in biochemistry and biophysics.
650 0 $aBinding sites (Biochemistry)$xThermodynamics.$0http://id.loc.gov/authorities/subjects/sh95002899
650 0 $aLigand binding (Biochemistry)$xThermodynamics.$0http://id.loc.gov/authorities/subjects/sh95002902
650 0 $aCooperative binding (Biochemistry)$xThermodynamics.$0http://id.loc.gov/authorities/subjects/sh95002903
650 0 $aMacromolecules$xThermodynamics.
650 2 $aBinding Sites.$0https://id.nlm.nih.gov/mesh/D001665
650 2 $aBiochemistry.$0https://id.nlm.nih.gov/mesh/D001671
650 2 $aThermodynamics.$0https://id.nlm.nih.gov/mesh/D013816
852 00 $boff,hsl$hQP517.B42$iD5 1995