The Unfolded State of NTL9 Is Compact in the Absence of Denaturant-Reference-Cited by-同舟云学术

The Unfolded State of NTL9 Is Compact in the Absence of Denaturant

Published:2006-07-27 Issue:33 Volume:45 Page:10110-10116
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Anil Burcu¹,Li Ying¹,Cho Jae-Hyun¹,Raleigh Daniel P.¹

Affiliation:

1. Department of Chemistry, State University of New York, Stony Brook, New York 11794-3400, Graduate Program in Biochemistry and Structural Biology, State University of New York, Stony Brook, New York 11794, and Graduate Program in Biophysics, State University of New York, Stony Brook, New York 11794

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi060636o

Reference33 articles.

1. Protein folding mechanisms: new methods and emerging ideas

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