Structure and Stability of the N-Terminal Domain of the Ribosomal Protein L9: Evidence for Rapid Two-State Folding-Reference-Cited by-同舟云学术

Structure and Stability of the N-Terminal Domain of the Ribosomal Protein L9: Evidence for Rapid Two-State Folding

Published:1998-01-01 Issue:4 Volume:37 Page:1025-1032
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kuhlman Brian¹,Boice Judith A.¹,Fairman Robert¹,Raleigh Daniel P.¹

Affiliation:

1. Department of Chemistry and Graduate Programs in Biophysics and in Molecular and Cellular Biology, State University of New York at Stony Brook, Stony Brook, New York 11794-3400, Bristol-Myers Squibb Pharmaceutical Research Institute, P.O. Box 4000, Princeton, New Jersey 08543-4000, and Department of Molecular, Cell and Developmental Biology, Haverford College, Haverford, Pennsylvania 19041

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi972352x

Reference49 articles.

1. Crystal structure of prokaryotic ribosomal protein L9: a bi-lobed RNA-binding protein.

2. Ribosomal Protein L9: A Structure Determination by the Combined Use of X-ray Crystallography and NMR Spectroscopy

3. RNA—protein complexes

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