Physical studies of tyrosine and tryptophan residues in mammalian A1 heterogeneous nuclear ribonucleoprotein Support for a segmented structure-Reference-Cited by-同舟云学术

Physical studies of tyrosine and tryptophan residues in mammalian A1 heterogeneous nuclear ribonucleoprotein Support for a segmented structure

Published:1991-09 Issue:2 Volume:221 Page:693-709
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Casas-Finet JoséR.,Karpel Richard L.,Maki August H.,Kumar Amalendra,Wilson Samuel H.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference62 articles.

1. Refined structure of the gene 5 DNA binding protein from bacteriophage fd;Brayer;J. Mol. Biol.,1983

2. Primary structure of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts;Burd,1989

3. Role of tryptophan and cysteine in the binding of gene 32 protein from phage T4 to single-stranded DNA. Modification of crucial residues by oxidation with selective free radical anions;Casas-Finet;Biochemistry,1984

4. Tryptophan 54 and phenylalanine 60 are involved synergistically in the binding of E. coli SSB protein to single-stranded polynucleotides;Casas-Finet;FEBS Letters,1987

5. Optically detected magnetic resonance of tryptophan residues in Escherichia coli ssb gene product and E. coli plasmid-encoded single-stranded DNA-binding proteins, and their complexes with poly(deoxythymidylic) acid;Casas-Finet;J. Biol. Chem.,1987

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