The Perturbation of Tryptophan Fluorescence by Phenylalanine to Alanine Mutations Identifies the Hydrophobic Core in a Subset of Bacterial Ig-like Domains
Author:
Affiliation:
1. Centre for Cellular and Molecular Biology (CCMB), CSIR, Uppal Road, Hyderabad 500 007, India
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi400128r
Reference15 articles.
1. Pathogenic Leptospira species express surface-exposed proteins belonging to the bacterial immunoglobulin superfamily
2. Calcium Binds to Leptospiral Immunoglobulin-like Protein, LigB, and Modulates Fibronectin Binding
3. Repeated Domains of Leptospira Immunoglobulin-like Proteins Interact with Elastin and Tropoelastin
4. Big Domains Are Novel Ca2+-Binding Modules: Evidences from Big Domains of Leptospira Immunoglobulin-Like (Lig) Proteins
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1. Crystal structure of a variable region segment of Leptospira host-interacting outer surface protein, LigA, reveals the orientation of Ig-like domains;International Journal of Biological Macromolecules;2023-07
2. Comparative screening of recombinant antigen thermostability for improved leptospirosis vaccine design;Biotechnology and Bioengineering;2018-12-05
3. Leptospira Immunoglobulin-Like Protein B (LigB) Binds to Both the C-Terminal 23 Amino Acids of Fibrinogen αC Domain and Factor XIII: Insight into the Mechanism of LigB-Mediated Blockage of Fibrinogen α Chain Cross-Linking;PLOS Neglected Tropical Diseases;2016-09-13
4. NMR Solution Structure of the Terminal Immunoglobulin-like Domain from the Leptospira Host-Interacting Outer Membrane Protein, LigB;Biochemistry;2014-08-04
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