Disentangling the Coil: Modulation of Conformational and Dynamic Properties by Site-Directed Mutation in the Non-Native State of Hen Egg White Lysozyme-Reference-Cited by-同舟云学术

Disentangling the Coil: Modulation of Conformational and Dynamic Properties by Site-Directed Mutation in the Non-Native State of Hen Egg White Lysozyme

Published:2012-04-13 Issue:16 Volume:51 Page:3361-3372
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sziegat Friederike¹,Silvers Robert¹,Hähnke Martin¹,Jensen Malene Ringkjøbing²,Blackledge Martin²,Wirmer-Bartoschek Julia¹,Schwalbe Harald¹

Affiliation:

1. Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance (BMRZ), Johann Wolfgang Goethe-University, Frankfurt a. M., Max-von-Laue-Straße 7, D-60438 Frankfurt, Germany

2. Protein Dynamics and Flexibility by NMR, Institut de Biologie Structurale Jean-Pierre Ebel, CEA-CNRS-UJF UMR 5075, 41 Rue Jules Horowitz, Grenoble 38027, France

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi300222f

Reference63 articles.

1. Protein folding and misfolding

2. Protein Folding Handbook

3. Structural and Dynamical Properties of a Denatured Protein. Heteronuclear 3D NMR Experiments and Theoretical Simulations of Lysozyme in 8 M Urea

4. Long-Range Interactions Within a Nonnative Protein

5. Modulation of Compactness and Long-Range Interactions of Unfolded Lysozyme by Single Point Mutations

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