Quenching of alkaline phosphatase phosphorescence by O2 and NO. Evidence for inflexible regions of protein structure-Reference-Cited by-同舟云学术

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Quenching of alkaline phosphatase phosphorescence by O2 and NO. Evidence for inflexible regions of protein structure

Published:1987-07 Issue:1 Volume:52 Page:23-28
ISSN:0006-3495
Container-title:Biophysical Journal
language:en
Short-container-title:Biophysical Journal

Author:

Strambini G.B.

Publisher

Elsevier BV

Subject

Biophysics

Cited by 66 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Stereoselective Binding of Flurbiprofen Enantiomers and their Methyl Esters to Human Serum Albumin Studied by Time-Resolved Phosphorescence;Chirality;2012-06-21

2. Influence of Denaturants on Native-State Structural Fluctuations in Azurin Probed by Molecular Size-Dependent Quenching of Trp Phosphorescence;The Journal of Physical Chemistry B;2011-10-28

3. Protein dynamics and pressure: What can high pressure tell us about protein structural flexibility?;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2011-08

4. Amplitude Spectrum of Structural Fluctuations in Proteins from the Internal Diffusion of Solutes of Increasing Molecular Size: A Trp Phosphorescence Quenching Study;Biochemistry;2011-02-15

5. Acrylonitrile Quenching of Trp Phosphorescence in Proteins: A Probe of the Internal Flexibility of the Globular Fold;Biophysical Journal;2010-08

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