Biophysics

Receptor binding, immune escape, and protein stability direct the natural selection of SARS-CoV-2 variants

1. Vaibhav Upadhyay
2. Alexandra Lucas
3. Sudipta Panja
4. Ryuki Miyauchi
5. Krishna M.G. Mallela

Reviewed by ScreenIT

Cooperative multivalent receptor binding promotes exposure of the SARS-CoV-2 fusion machinery core

1. Alexander J. Pak
2. Alvin Yu
3. Zunlong Ke
4. John A. G. Briggs
5. Gregory A. Voth

Reviewed by ScreenIT

Structure and Dynamics of RNA Guanine Quadruplexes in SARS-CoV-2 Genome. Original Strategies against Emerging Viruses

1. Tom Miclot
2. Cécilia Hognon
3. Emmanuelle Bignon
4. Alessio Terenzi
5. Marco Marazzi
6. Giampaolo Barone
7. Antonio Monari

Reviewed by ScreenIT

Water-Triggered, Irreversible Conformational Change of SARS-CoV-2 Main Protease on Passing from the Solid State to Aqueous Solution

1. Narjes Ansari
2. Valerio Rizzi
3. Paolo Carloni
4. Michele Parrinello

Reviewed by ScreenIT

Role of ATP in the RNA Translocation Mechanism of SARS-CoV-2 NSP13 Helicase

1. Ryan Weber
2. Martin McCullagh

Reviewed by ScreenIT

Fluorescence signatures of SARS-CoV-2 spike S1 proteins and a human ACE-2: excitation-emission maps and fluorescence lifetimes

1. Jonas Grzesiak
2. Lea Fellner
3. Karin Grünewald
4. Christoph Kölbl
5. Arne Walter
6. Reinhold Horlacher
7. Frank Duschek

Reviewed by ScreenIT

Landscape-Based Mutational Sensitivity Cartography and Network Community Analysis of the SARS-CoV-2 Spike Protein Structures: Quantifying Functional Effects of the Circulating D614G Variant

1. Gennady M. Verkhivker
2. Steve Agajanian
3. Deniz Yasar Oztas
4. Grace Gupta

Reviewed by ScreenIT

Presence of a SARS-COV-2 protein enhances Amyloid Formation of Serum Amyloid A

1. Asis K. Jana
2. Augustus B. Greenwood
3. Ulrich H. E. Hansmann

Reviewed by ScreenIT

Molecular rationale for SARS-CoV-2 spike circulating mutations able to escape bamlanivimab and etesevimab monoclonal antibodies

1. Erik Laurini
2. Domenico Marson
3. Suzana Aulic
4. Alice Fermeglia
5. Sabrina Pricl

Reviewed by ScreenIT

Structural intermediates observed only in intact Escherichia coli indicate a mechanism for TonB-dependent transport

1. Thushani D Nilaweera
2. David A Nyenhuis
3. David S Cafiso

• Curated by eLife

  Evaluation Summary:

  The manuscript endeavors to explain the mechanism of action of the gram-negative bacterial outer membrane TonB-dependent transporter BtuB, which acquires vitamin B12 from the external environment. The authors use electron paramagnetic resonance spectroscopy to monitor the proximity of different parts of this protein to one another during the binding of B12 directly in the E. coli outer membrane. This manuscript will be of interest to those who study the biophysics of membrane transporters and stresses the importance of studying membrane proteins in their native environment.

  (This preprint has been reviewed by eLife. We include the public reviews from the reviewers here; the authors also receive private feedback with suggested changes to the manuscript. Reviewer #2 and Reviewer #3 agreed to share their names with the authors.)

Reviewed by eLife