Measurement of structural and free energy changes in hemoglobin by hydrogen exchange methods

Author: Englander, S.W.

Description: Porphyrins are very generally found in the company of proteins, and a lot of effort has been devoted to finding out how they interact. Many studies have focused on three-dimensional structure and change in three-dimensional structure. Such studies have supplied important parts of the picture; but also fundamental in these interactions are the energy relationships, and about these we know very little … The functional impact of any structure change, its contribution to allosteric signal transmission and to modification of protein function, can only be ascertained by measuring quantitatively its free energy content

Subject headings: Animals; Hemoglobins; Hydrogen; Kinetics; Ligands; Mathematics; Oxyhemoglobins; Protein Conformation; Protein Denaturation; Thermodynamics; Time Factors; Tritium

Publication year: 1975

Journal or book title: Annals of the New York Academy of Sciences

Volume: 244

Issue: 1

Pages: 10-27

Find the full text: https://nyaspubs.onlinelibrary.wiley.com/doi/abs/10.1111/j.1749-6632.1975.tb41518.x

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Type: Journal Article

Serial number: 2869