Literature DB >> 4361855

Magnetic resonance studies of human hemoglobins and their implications to the structure-function relationships in human normal and abnormal hemoglobins.

C Ho, T R Lindstrom, J J Baldassare, J J Breen.   

Abstract

Entities:  

Mesh:

Substances:

Year:  1973        PMID: 4361855     DOI: 10.1111/j.1749-6632.1973.tb15250.x

Source DB:  PubMed          Journal:  Ann N Y Acad Sci        ISSN: 0077-8923            Impact factor:   5.691


× No keyword cloud information.
  4 in total

1.  The physical state of water and ions in living cells and a new theory of the energization of biological work performance by ATP.

Authors:  G N Ling
Journal:  Mol Cell Biochem       Date:  1977-05-03       Impact factor: 3.396

2.  Probing the energetics of proteins through structural perturbation: sites of regulatory energy in human hemoglobin.

Authors:  D W Pettigrew; P H Romeo; A Tsapis; J Thillet; M L Smith; B W Turner; G K Ackers
Journal:  Proc Natl Acad Sci U S A       Date:  1982-03       Impact factor: 11.205

3.  A proton nuclear magnetic resonance investigation of proximal histidyl residues in human normal and abnormal hemoglobins. A probe for the heme pocket.

Authors:  S Takahashi; A K Lin; C Ho
Journal:  Biophys J       Date:  1982-07       Impact factor: 4.033

4.  Nuclear magnetic resonance study of heme-heme interaction in hemoglobin M Milwaukee: implications concerning the mechanism of cooperative ligand binding in normal hemoglobin.

Authors:  L W Fung; A P Minton; C Ho
Journal:  Proc Natl Acad Sci U S A       Date:  1976-05       Impact factor: 11.205

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.