Estimation of the Distance Change between Cysteine-457 and the Nucleotide Binding Site When Sodium Pump Changes Conformation from E1 to E2 by Fluorescence Energy Transfer Measurements-Reference-Cited by-同舟云学术

Estimation of the Distance Change between Cysteine-457 and the Nucleotide Binding Site When Sodium Pump Changes Conformation from E1 to E2 by Fluorescence Energy Transfer Measurements

Published:1996-01-01 Issue:25 Volume:35 Page:8419-8428
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lin Shwu-Hwa¹,Faller Larry D.¹

Affiliation:

1. Center for Ulcer Research and Education, Department of Medicine, University of California at Los Angeles School of Medicine, and Wadsworth Division, Department of Veterans Affairs Medical Center, West Los Angeles, California 90073

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi960407%2B

Reference49 articles.

1. Structural dynamics and oligomeric interactions of Na+,K(+)-ATPase as monitored using fluorescence energy transfer

2. The carbohydrate moieties of the beta-subunit of Na+, K(+)-ATPase: their lateral motions and proximity to the cardiac glycoside site

3. The active site structure of Na+- and K+-stimulated ATPase. Location of a specific fluorescein isothiocyanate reactive site.

4. Proteolytic fragmentation of the catalytic subunit of the sodium and potassium adenosine triphosphatase. Alignment of tryptic and chymotryptic fragments and location of sites labeled with ATP and iodoacetate

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