Structural consequences of cutting a binding loop: two circularly permuted variants of streptavidin-Reference-Cited by-同舟云学术

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Structural consequences of cutting a binding loop: two circularly permuted variants of streptavidin

Published:2013-05-11 Issue:6 Volume:69 Page:968-977
ISSN:0907-4449
Container-title:Acta Crystallographica Section D Biological Crystallography
language:
Short-container-title:Acta Crystallogr D Biol Cryst

Author:

Le Trong Isolde,Chu Vano,Xing Yi,Lybrand Terry P.,Stayton Patrick S.,Stenkamp Ronald E.

Publisher

International Union of Crystallography (IUCr)

Subject

General Medicine,Structural Biology

Link

http://journals.iucr.org/d/issues/2013/06/00/be5218/be5218.pdf

Reference56 articles.

1. Ion-water interaction potentials derived from free energy perturbation simulations

2. A Distal Point Mutation in the Streptavidin−Biotin Complex Preserves Structure but Diminishes Binding Affinity: Experimental Evidence of Electronic Polarization Effects?

3. Second-Contact Shell Mutation Diminishes Streptavidin–Biotin Binding Affinity through Transmitted Effects on Equilibrium Dynamics

4. The missing term in effective pair potentials

5. The Protein Data Bank

Cited by 5 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. Engineering a disulfide-gated switch in streptavidin enables reversible binding without sacrificing binding affinity;Scientific Reports;2020-07-27

2. The Role of the Active Site Flap in Streptavidin/Biotin Complex Formation;Journal of the American Chemical Society;2018-04-02

3. How Diverse Are the Protein-Bound Conformations of Small-Molecule Drugs and Cofactors?;Frontiers in Chemistry;2018-03-27

4. A simple approach for preparation of affinity matrices: Simultaneous purification and reversible immobilization of a streptavidin mutein to agarose matrix;Scientific Reports;2017-02-21

5. Love–Hate ligands for high resolution analysis of strain in ultra-stable protein/small molecule interaction;Bioorganic & Medicinal Chemistry;2014-10

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