✦ LIBER ✦

Heat capacity of proteins: II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: Protein unfolding effects

✍ Scribed by P.L. Privalov; G.I. Makhatadze

Book ID: 119443266
Publisher: Elsevier Science
Year: 1990
Tongue: English
Weight: 564 KB
Volume: 213
Category: Article
ISSN: 0022-2836
DOI: 10.1016/s0022-2836(05)80198-6

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Contribution of hydration and non-covale

Contribution of hydration and non-covalent interactions to the heat capacity effect on protein unfolding

✍ Peter L. Privalov; George I. Makhatadze 📂 Article 📅 1992 🏛 Elsevier Science 🌐 English ⚖ 905 KB

Heat capacity of proteins: I. Partial mo

Heat capacity of proteins: I. Partial molar heat capacity of individual amino acid residues in aqueous solution: Hydration effect

✍ G.I. Makhatadze; P.L. Privalov 📂 Article 📅 1990 🏛 Elsevier Science 🌐 English ⚖ 880 KB

Contribution of secondary structure to t

Contribution of secondary structure to the heat capacity and enthalpy distribution of the unfolded state in proteins

✍ Douglas Poland 📂 Article 📅 2001 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 142 KB 👁 1 views

## Abstract We have recently shown that one can construct the enthalpy distribution for protein molecules from experimental knowledge of the temperature dependence of the heat capacity. For many proteins the enthalpy distribution evaluated at the midpoint of the denaturation transition (correspondi

Toward the Physical Basis of Thermophili

Toward the Physical Basis of Thermophilic Proteins: Linking of Enriched Polar Interactions and Reduced Heat Capacity of Unfolding

✍ Zhou, Huan-Xiang 📂 Article 📅 2002 🏛 Biophysical Society 🌐 English ⚖ 209 KB

Direct Detection of Heat and Cold Denatu

Direct Detection of Heat and Cold Denaturation for Partial Unfolding of a Protein

✍ Nelson, Carma J.; LaConte, Michael J.; Bowler, Bruce E. 📂 Article 📅 2001 🏛 American Chemical Society 🌐 English ⚖ 47 KB

Glucosylation of β-lactoglobulin lowers

Glucosylation of β-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics

✍ Annemarie M.M. Van Teeffelen; Kerensa Broersen; Harmen H.J. de Jongh 📂 Article 📅 2005 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 337 KB