Kinetics and Motional Dynamics of Spin-Labeled Yeast Iso-1-cytochrome c: 1. Stopped-Flow Electron Paramagnetic Resonance as a Probe for Protein Folding/Unfolding of the C-Terminal Helix Spin-Labeled at Cysteine 102-Reference-Cited by-同舟云学术

Kinetics and Motional Dynamics of Spin-Labeled Yeast Iso-1-cytochrome c: 1. Stopped-Flow Electron Paramagnetic Resonance as a Probe for Protein Folding/Unfolding of the C-Terminal Helix Spin-Labeled at Cysteine 102

Published:1997-03-01 Issue:10 Volume:36 Page:2884-2897
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Qu Kunbin¹,Vaughn Jeffrey L.¹,Sienkiewicz Andrzej¹,Scholes Charles P.¹,Fetrow Jacquelyn S.¹

Affiliation:

1. Departments of Chemistry, Physics, and Biological Sciences, Center for Biophysics and Biochemistry, State University of New York at Albany, Albany, New York 12222, and Institute of Physics of the Polish Academy of Sciences, Al. Lotnikov 32/46, 02668 Warsaw, Poland

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi962155i

Reference79 articles.

1. Constraints on amino acid substitutions in the N-terminal helix of cytochrome c explored by random mutagenesis

Cited by 64 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. Structural Flexibility of Tau in Its Interaction with Microtubules as Viewed by Site-Directed Spin Labeling EPR Spectroscopy;Methods in Molecular Biology;2024

2. Enzyme Immobilization on Graphite Oxide (GO) Surface via One-Pot Synthesis of GO/Metal–Organic Framework Composites for Large-Substrate Biocatalysis;ACS Applied Materials & Interfaces;2020-04-27

3. Site-selective protein modification via disulfide rebridging for fast tetrazine/trans-cyclooctene bioconjugation;Organic & Biomolecular Chemistry;2020

4. Using Paramagnetic Probes to Study Structural Transitions in Proteins;Electron Paramagnetic Resonance Spectroscopy;2020

5. Effect of a Paramagnetic Spin Label on the Intrinsically Disordered Peptide Ensemble of Amyloid-β;Biophysical Journal;2017-09