Use of the Novel Fluorescent Amino Acid p-Cyanophenylalanine Offers a Direct Probe of Hydrophobic Core Formation during the Folding of the N-Terminal Domain of the Ribosomal Protein L9 and Provides Evidence for Two-State Folding-Reference-Cited by-同舟云学术

Use of the Novel Fluorescent Amino Acid p-Cyanophenylalanine Offers a Direct Probe of Hydrophobic Core Formation during the Folding of the N-Terminal Domain of the Ribosomal Protein L9 and Provides Evidence for Two-State Folding

Published:2007-10-01 Issue:43 Volume:46 Page:12308-12313
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Aprilakis Konstantinos N.¹,Taskent Humeyra¹,Raleigh Daniel P.¹

Affiliation:

1. Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400, Institute for Chemical Biology and Drug Discovery, State University of New York at Stony Brook, Stony Brook, New York 11794-3400, and Graduate Program in Biochemistry and Structural Biology, State University of New York at Stony Brook, Stony Brook, New York 11794-3400

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi7010674

Reference32 articles.

1. Are there pathways for protein folding?

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