Protein heat capacity reflects the dynamics of enthalpy exchange between the single macromolecule and the surroundings

scientific article published in January 2000

Protein heat capacity reflects the dynamics of enthalpy exchange between the single macromolecule and the surroundings is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/1097-0134(2000)41:4+<86::AID-PROT80>3.0.CO;2-U
P698PubMed publication ID11013403

P2093author name stringHinz HJ
Hallerbach B
P2860cites workAn alternative interpretation of the heat capacity changes associated with protein unfoldingQ33484598
Thermodynamic fluctuations in protein moleculesQ35016394
Study of strong to ultratight protein interactions using differential scanning calorimetryQ37951616
Protein fluctuations and the thermodynamic uncertainty principleQ40194572
The control of protein stability and association by weak interactions with water: how do solvents affect these processes?Q40833005
Validity of the "two-state" hypothesis for conformational transitions of proteinsQ41527044
On thermal transitions in biological macromoleculesQ47901259
5 The determination of the partial specific volume of proteins by the mechanical oscillator techniqueQ47906030
Scanning microcalorimetry in studying temperature-induced changes in proteinsQ52651402
Response functions of proteinsQ73345570
Protein heat capacity: inconsistencies in the current view of cold denaturationQ79207658
The 'Janus' nature of proteins: systems at the verge of the microscopic and macroscopic worldQ79213326
P407language of work or nameEnglishQ1860
P921main subjectmacromoleculeQ178593
P304page(s)86-92
P577publication date2000-01-01
P1433published inProteinsQ7251514
P1476titleProtein heat capacity reflects the dynamics of enthalpy exchange between the single macromolecule and the surroundings
P478volumeSuppl 4

Reverse relations

cites work (P2860)
Q40305051Heat capacity changes associated with DNA duplex formation: salt- and sequence-dependent effects
Q40304948Salt-dependent heat capacity changes for RNA duplex formation

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