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Literature DB >> 24739154

The importance of intrinsic order in a disordered protein ligand.

Natalie K Goto¹.

Abstract

Entities: Disease

Mesh：

Substances：

Year: 2014 PMID： 24739154 PMCID： PMC4008830 DOI： 10.1016/j.bpj.2014.03.005

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

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15 in total

1. Characterization of the conformational equilibrium between the two major substates of RNase A using NMR chemical shifts.

Authors: Carlo Camilloni; Paul Robustelli; Alfonso De Simone; Andrea Cavalli; Michele Vendruscolo
Journal: J Am Chem Soc Date: 2012-02-22 Impact factor: 15.419

2. Coupled folding and binding with alpha-helix-forming molecular recognition elements.

Authors: Christopher J Oldfield; Yugong Cheng; Marc S Cortese; Pedro Romero; Vladimir N Uversky; A Keith Dunker
Journal: Biochemistry Date: 2005-09-20 Impact factor: 3.162

3. Mechanism of induced folding: Both folding before binding and binding before folding can be realized in staphylococcal nuclease mutants.

Authors: Masayoshi Onitsuka; Hironari Kamikubo; Yoichi Yamazaki; Mikio Kataoka
Journal: Proteins Date: 2008-08-15

4. Compaction properties of an intrinsically disordered protein: Sic1 and its kinase-inhibitor domain.

Authors: Stefania Brocca; Lorenzo Testa; Frank Sobott; Maria Samalikova; Antonino Natalello; Elena Papaleo; Marina Lotti; Luca De Gioia; Silvia Maria Doglia; Lilia Alberghina; Rita Grandori
Journal: Biophys J Date: 2011-05-04 Impact factor: 4.033

5. Assessment of the use of NMR chemical shifts as replica-averaged structural restraints in molecular dynamics simulations to characterize the dynamics of proteins.

Authors: Carlo Camilloni; Andrea Cavalli; Michele Vendruscolo
Journal: J Phys Chem B Date: 2013-02-01 Impact factor: 2.991

Review 2. Information flow and protein dynamics: the interplay between nuclear magnetic resonance spectroscopy and molecular dynamics simulations.

Authors: Nina Pastor; Carlos Amero
Journal: Front Plant Sci Date: 2015-05-05 Impact factor: 5.753

2 in total

The importance of intrinsic order in a disordered protein ligand.

1. Characterization of the conformational equilibrium between the two major substates of RNase A using NMR chemical shifts.

2. Coupled folding and binding with alpha-helix-forming molecular recognition elements.

3. Mechanism of induced folding: Both folding before binding and binding before folding can be realized in staphylococcal nuclease mutants.

4. Compaction properties of an intrinsically disordered protein: Sic1 and its kinase-inhibitor domain.

5. Assessment of the use of NMR chemical shifts as replica-averaged structural restraints in molecular dynamics simulations to characterize the dynamics of proteins.

6. Solution model of the intrinsically disordered polyglutamine tract-binding protein-1.

7. Intrinsic protein disorder in complete genomes.

8. NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein.

9. Distinct binding modes of two epitopes in Gab2 that interact with the SH3C domain of Grb2.

10. Internal dynamics control activation and activity of the autoinhibited Vav DH domain.

1. Reply to: "Only kinetics can prove conformational selection".

Review 2. Information flow and protein dynamics: the interplay between nuclear magnetic resonance spectroscopy and molecular dynamics simulations.