Evidence for the residual tertiary structure in the urea-unfolded form of bacteriophage T5 endolysin-Reference-Cited by-同舟云学术

Evidence for the residual tertiary structure in the urea-unfolded form of bacteriophage T5 endolysin

Published:2016-05-20 Issue:6 Volume:35 Page:1331-1338
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Kutyshenko Victor P.¹,Prokhorov Dmitry A.¹,Mikoulinskaia Galina V.²,Molochkov Nikolai V.¹,Paskevich Svetlana I.¹,Uversky Vladimir N.³⁴

Affiliation:

1. Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia

2. Branch of Shemyakin & Ovchinnikov’s Institute of Bioorganic Chemistry, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russia

3. Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, USA

4. Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, Tikhoretsky Ave. 4, St. Petersburg 194064, Russia

Funder

Russian Foundation for Basic Research

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2016.1182948

Reference32 articles.

1. Principles that Govern the Folding of Protein Chains

2. Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy

3. TOP-IDP-Scale: A New Amino Acid Scale Measuring Propensity for Intrinsic Disorder