Substrate Recognition and Saturation Kinetics in de Novo Designed Histidine-Based Four-Helix Bundle Catalysts

1998 ◽  
Vol 120 (40) ◽  
pp. 10287-10295 ◽  
Author(s):  
Kerstin S. Broo ◽  
Helena Nilsson ◽  
Jonas Nilsson ◽  
Lars Baltzer
Keyword(s):  
De Novo ◽  
Substrate Recognition ◽  
Helix Bundle ◽  
Saturation Kinetics ◽  
Four Helix Bundle

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 Inside Cover: De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four-Helix Bundle Hemeprotein (Chem. Eur. J. 50/2012)

2012 ◽  
Vol 18 (50) ◽  
pp. 15890-15890
Author(s):  
Marina Faiella ◽  
Ornella Maglio ◽  
Flavia Nastri ◽  
Angela Lombardi ◽  
Liliana Lista ◽  
...  
Keyword(s):  
De Novo ◽  
De Novo Design ◽  
Design Synthesis ◽  
Helix Bundle ◽  
Four Helix Bundle

Design of a Fe 4 S 4 cluster into the core of a de novo four‐helix bundle

2020 ◽  
Vol 67 (4) ◽  
pp. 574-585 ◽  
Author(s):  
Joshua A. Mancini ◽  
Douglas H. Pike ◽  
Alexei M. Tyryshkin ◽  
Liti Haramaty ◽  
Michael S. Wang ◽  
...  
Keyword(s):  
De Novo ◽  
Helix Bundle ◽  
The Core ◽  
Four Helix Bundle

Artificial Diiron Enzymes with a De Novo Designed Four-Helix Bundle Structure

2015 ◽  
Vol 2015 (21) ◽  
pp. 3352-3352 ◽  
Author(s):  
Marco Chino ◽  
Ornella Maglio ◽  
Flavia Nastri ◽  
Vincenzo Pavone ◽  
William F. DeGrado ◽  
...  
Keyword(s):  
De Novo ◽  
Helix Bundle ◽  
Four Helix Bundle ◽  
Diiron Enzymes ◽  
Bundle Structure

De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence

Science ◽  
1990 ◽  
Vol 249 (4971) ◽  
pp. 884-891 ◽  
Author(s):  
M. Hecht ◽  
J. Richardson ◽  
D. Richardson ◽  
R. Ogden
Keyword(s):  
De Novo ◽  
De Novo Design ◽  
Helix Bundle ◽  
Four Helix Bundle ◽  
Bundle Protein

scholarly journals Oxygen Reactivity of the Biferrous Site in the de novo Designed Four Helix Bundle Peptide DFsc: Nature of the “Intermediate” and Reaction Mechanism

2008 ◽  
Vol 130 (29) ◽  
pp. 9188-9189 ◽  
Author(s):  
Jennifer R. Calhoun ◽  
Caleb B. Bell ◽  
Thomas J. Smith ◽  
Thomas J. Thamann ◽  
William F. DeGrado ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
De Novo ◽  
Helix Bundle ◽  
Four Helix Bundle ◽  
Oxygen Reactivity

scholarly journals De Novo Design of Four-Helix Bundle Metalloproteins: One Scaffold, Diverse Reactivities

2019 ◽  
Author(s):  
Angela Lombardi ◽  
Fabio Pirro ◽  
Ornella Maglio ◽  
Marco Chino ◽  
William F. DeGrado
Keyword(s):  
De Novo ◽  
De Novo Design ◽  
Helix Bundle ◽  
Four Helix Bundle

scholarly journals Computational De Novo Design and Characterization of a Four-Helix Bundle Protein that Selectively Binds a Nonbiological Cofactor [J.Am. Chem. Soc.2005,127, 1346−1347].

2006 ◽  
Vol 128 (2) ◽  
pp. 663-663 ◽  
Author(s):  
Frank V. Cochran ◽  
Sophia P. Wu ◽  
Wei Wang ◽  
Vikas Nanda ◽  
Jeffery G. Saven ◽  
...  
Keyword(s):  
De Novo ◽  
De Novo Design ◽  
Helix Bundle ◽  
Four Helix Bundle ◽  
Bundle Protein

De Novo Design, Expression and Characterization of Felix: A Four-Helix Bundle Protein of Native-Like Sequence

Science ◽  
1990 ◽  
pp. 973-973
Author(s):  
M. H. Hecht ◽  
J. H. Richardson ◽  
D. C. Richardson ◽  
R. C. Ogden
Keyword(s):  
De Novo ◽  
De Novo Design ◽  
Helix Bundle ◽  
Four Helix Bundle ◽  
Bundle Protein

scholarly journals Computational de novo design of a four-helix bundle protein-DND_4HB

2014 ◽  
Vol 24 (4) ◽  
pp. 434-445 ◽  
Author(s):  
Grant S. Murphy ◽  
Bharatwaj Sathyamoorthy ◽  
Bryan S. Der ◽  
Mischa C. Machius ◽  
Surya V. Pulavarti ◽  
...  
Keyword(s):  
De Novo ◽  
De Novo Design ◽  
Helix Bundle ◽  
Four Helix Bundle ◽  
Bundle Protein
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