Work

Site mutations disrupt inter-helical H-bonds (α14W–α67T and β15W–β72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation

Year: 2002

Type: article

Source: Biophysical Chemistry

DOI: 10.1016/s0301-4622(02)00274-0

Authors: Ching-Hsuan Tsai, Virgil Simplaceanu, Nancy T. Ho, Tong-Jian Shen, Daojing Wang, Thomas G. Spiro, Chien Ho

Institutions: Carnegie Mellon University, Princeton University

Language: English

Topic: Hemoglobin structure and function

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: closed

Funders: National Institutes of Health, National Heart, Lung, and Blood Institute, National Institute of General Medical Sciences, National Center for Research Resources

Awards: MOLECULAR CONTROLS OF HEMOGLOBIN FUNCTION, G1703958519, G1924805489, G4539068250, G5604735104, BIOPHYSICAL &MOLECULAR BIOLOGICAL STUDIES OF HEMOGLOBIN, PURCHASE OF A 600-MHZ NMR SPECTROMETER, Ultraviolet Raman Spectroscopic Studies of Protein Dynamics

OpenAlex ID: W2081524633

FWCI: 0.571

Cites: 44

Cited by: 6

Related to: 10