Protein Folding Dynamics:  Application of the Diffusion-Collision Model to the Folding of a Four-Helix Bundle

1996 ◽  
Vol 100 (7) ◽  
pp. 2498-2509 ◽  
Author(s):  
Kanthi K. Yapa ◽  
David L. Weaver
Keyword(s):  
Protein Folding ◽  
Collision Model ◽  
Helix Bundle ◽  
Folding Dynamics ◽  
Four Helix Bundle

Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis

FEBS Letters ◽  
2007 ◽  
Vol 581 (25) ◽  
pp. 4965-4971 ◽  
Author(s):  
Kristofer Modig ◽  
Vibeke W. Jürgensen ◽  
Kresten Lindorff-Larsen ◽  
Wolfgang Fieber ◽  
Henrik G. Bohr ◽  
...  
Keyword(s):  
Protein Folding ◽  
Chemical Shift ◽  
Helix Bundle ◽  
Shift Analysis ◽  
Four Helix Bundle ◽  
Chemical Shift Analysis

scholarly journals Rational thermostabilisation of four-helix bundle dimeric de novo proteins

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Shin Irumagawa ◽  
Kaito Kobayashi ◽  
Yutaka Saito ◽  
Takeshi Miyata ◽  
Mitsuo Umetsu ◽  
...  
Keyword(s):  
Protein Design ◽  
De Novo ◽  
Protein Complexes ◽  
Salt Bridge ◽  
Dynamics Simulation ◽  
Saturation Mutagenesis ◽  
Helix Bundle ◽  
Stable Mutant ◽  
Four Helix Bundle ◽  
The Stability

AbstractThe stability of proteins is an important factor for industrial and medical applications. Improving protein stability is one of the main subjects in protein engineering. In a previous study, we improved the stability of a four-helix bundle dimeric de novo protein (WA20) by five mutations. The stabilised mutant (H26L/G28S/N34L/V71L/E78L, SUWA) showed an extremely high denaturation midpoint temperature (Tm). Although SUWA is a remarkably hyperstable protein, in protein design and engineering, it is an attractive challenge to rationally explore more stable mutants. In this study, we predicted stabilising mutations of WA20 by in silico saturation mutagenesis and molecular dynamics simulation, and experimentally confirmed three stabilising mutations of WA20 (N22A, N22E, and H86K). The stability of a double mutant (N22A/H86K, rationally optimised WA20, ROWA) was greatly improved compared with WA20 (ΔTm = 10.6 °C). The model structures suggested that N22A enhances the stability of the α-helices and N22E and H86K contribute to salt-bridge formation for protein stabilisation. These mutations were also added to SUWA and improved its Tm. Remarkably, the most stable mutant of SUWA (N22E/H86K, rationally optimised SUWA, ROSA) showed the highest Tm (129.0 °C). These new thermostable mutants will be useful as a component of protein nanobuilding blocks to construct supramolecular protein complexes.

scholarly journals Effects of Energetic Heterogeneity on Protein Folding Dynamics Across Many Non-Homologous Proteins

2014 ◽  
Vol 106 (2) ◽  
pp. 673a
Author(s):  
Claude Sinner ◽  
Benjamin Lutz ◽  
Abhinav Verma ◽  
Alexander Schug
Keyword(s):  
Protein Folding ◽  
Homologous Proteins ◽  
Energetic Heterogeneity ◽  
Folding Dynamics

Self-Assembly of a Four-Helix Bundle on a DNA Quadruplex

2009 ◽  
Vol 48 (15) ◽  
pp. 2749-2751 ◽  
Author(s):  
Brooke A. Rosenzweig ◽  
Andrew D. Hamilton
Keyword(s):  
Self Assembly ◽  
Helix Bundle ◽  
Dna Quadruplex ◽  
Four Helix Bundle
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