Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Covalent chemistry on distended proteins.

Literature DB >> 16682625

Covalent chemistry on distended proteins.

Dennis E Discher¹, Nishant Bhasin, Colin P Johnson.

Abstract

Mesh：

Substances：
Proteins

Year: 2006 PMID： 16682625 PMCID： PMC1472479 DOI： 10.1073/pnas.0602388103

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

× No keyword cloud information.

13 in total

1. Pathway shifts and thermal softening in temperature-coupled forced unfolding of spectrin domains.

Authors: Richard Law; George Liao; Sandy Harper; Guoliang Yang; David W Speicher; Dennis E Discher
Journal: Biophys J Date: 2003-11 Impact factor: 4.033

2. Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering.

Authors: Susan B Fowler; Robert B Best; José L Toca Herrera; Trevor J Rutherford; Annette Steward; Emanuele Paci; Martin Karplus; Jane Clarke
Journal: J Mol Biol Date: 2002-09-27 Impact factor: 5.469

Review 3. Mechanical processes in biochemistry.

Authors: Carlos Bustamante; Yann R Chemla; Nancy R Forde; David Izhaky
Journal: Annu Rev Biochem Date: 2004 Impact factor: 23.643

4. Temperature softening of a protein in single-molecule experiments.

Authors: Michael Schlierf; Matthias Rief
Journal: J Mol Biol Date: 2005-10-10 Impact factor: 5.469

5. Transcription against an applied force.

Authors: H Yin; M D Wang; K Svoboda; R Landick; S M Block; J Gelles
Journal: Science Date: 1995-12-08 Impact factor: 47.728

6. Reversible unfolding of individual titin immunoglobulin domains by AFM.

Authors: M Rief; M Gautel; F Oesterhelt; J M Fernandez; H E Gaub
Journal: Science Date: 1997-05-16 Impact factor: 47.728

7. Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin.

Authors: O Mayans; J Wuerges; S Canela; M Gautel; M Wilmanns
Journal: Structure Date: 2001-04-04 Impact factor: 5.006

Covalent chemistry on distended proteins.

1. Pathway shifts and thermal softening in temperature-coupled forced unfolding of spectrin domains.

2. Mechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering.

Review 3. Mechanical processes in biochemistry.

4. Temperature softening of a protein in single-molecule experiments.

5. Transcription against an applied force.

6. Reversible unfolding of individual titin immunoglobulin domains by AFM.

7. Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin.

8. Chemistry on a single protein, vascular cell adhesion molecule-1, during forced unfolding.

9. Forced unfolding modulated by disulfide bonds in the Ig domains of a cell adhesion molecule.

10. Stepwise unfolding of titin under force-clamp atomic force microscopy.

Review 1. Molecular force transduction by ion channels: diversity and unifying principles.

2. Probing the effect of force on HIV-1 receptor CD4.

3. Shaping polymersomes into predictable morphologies via out-of-equilibrium self-assembly.