Ligand Preferences of Kringle 2 and Homologous Domains of Human Plasminogen: Canvassing Weak, Intermediate, and High-Affinity Binding Sites by 1H-NMR-Reference-Cited by-同舟云学术

Ligand Preferences of Kringle 2 and Homologous Domains of Human Plasminogen: Canvassing Weak, Intermediate, and High-Affinity Binding Sites by 1H-NMR

Published:1997-09-01 Issue:39 Volume:36 Page:11591-11604
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Marti Daniel N.¹,Hu Chih-Kao¹,An Seong Soo A.¹,von Haller Priska¹,Schaller Johann¹,Llinás Miguel¹

Affiliation:

1. Department of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, and Department of Chemistry and Biochemistry, University of Bern, CH-3012 Bern, Switzerland

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi971316v

Reference61 articles.

1. Solution structure of the kringle 4 domain from human plasminogen by 1H nuclear magnetic resonance spectroscopy and distance geometry

2. CHARMM: A program for macromolecular energy, minimization, and dynamics calculations

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