scholarly journals Designer proteins target flu

Nature ◽  
2011 ◽  
Vol 473 (7347) ◽  
pp. 256-257
Keyword(s):  
Designer Proteins

Molecular couturiers and designer proteins

1993 ◽  
Vol 11 (4) ◽  
pp. 111-114 ◽  
Author(s):  
M GEISOW
Keyword(s):  
Designer Proteins

scholarly journals Designer proteins activate fluorescent molecules

Nature ◽  
2018 ◽  
Vol 561 (7724) ◽  
pp. 471-472
Author(s):  
Roberto A. Chica
Keyword(s):  
Designer Proteins ◽  
Fluorescent Molecules

Ubiquitin Designer Proteins as a New Additive Generation toward Controlling Crystallization

2019 ◽  
Vol 141 (31) ◽  
pp. 12240-12245 ◽  
Author(s):  
Cristina Ruiz-Agudo ◽  
Joachim Lutz ◽  
Philipp Keckeis ◽  
Michael King ◽  
Andreas Marx ◽  
...  
Keyword(s):  
Designer Proteins

Designer proteins act as logic gates

Physics Today ◽  
2020 ◽  
Vol 73 (6) ◽  
pp. 17-19
Author(s):  
Heather M. Hill
Keyword(s):  
Logic Gates ◽  
Designer Proteins

Designer proteins produce potent HIV defense

Science ◽  
2015 ◽  
Vol 348 (6241) ◽  
pp. 1297-1297
Author(s):  
J. Cohen
Keyword(s):  
Designer Proteins

scholarly journals Expanding the space of protein geometries by computational design of de novo fold families

2020 ◽  
Author(s):  
Xingjie Pan ◽  
Michael Thompson ◽  
Yang Zhang ◽  
Lin Liu ◽  
James S. Fraser ◽  
...  
Keyword(s):  
De Novo ◽  
Design Method ◽  
Computational Design ◽  
Computational Method ◽  
Structural Elements ◽  
New Paradigm ◽  
Biophysical Characterization ◽  
Structure Space ◽  
Naturally Occurring ◽  
Designer Proteins

AbstractNaturally occurring proteins use a limited set of fold topologies, but vary the precise geometries of structural elements to create distinct shapes optimal for function. Here we present a computational design method termed LUCS that mimics nature’s ability to create families of proteins with the same overall fold but precisely tunable geometries. Through near-exhaustive sampling of loop-helix-loop elements, LUCS generates highly diverse geometries encompassing those found in nature but also surpassing known structure space. Biophysical characterization shows that 17 (38%) out of 45 tested LUCS designs were well folded, including 16 with designed non-native geometries. Four experimentally solved structures closely match the designs. LUCS greatly expands the designable structure space and provides a new paradigm for designing proteins with tunable geometries customizable for novel functions.One Sentence SummaryA computational method to systematically sample loop-helix-loop geometries expands the structure space of designer proteins.

scholarly journals Nonclassical nucleation of protein mesocrystals via oriented attachment

2020 ◽  
Author(s):  
Alexander E.S. Van Driessche ◽  
Nani Van Gerven ◽  
Rick R.M. Joosten ◽  
Wai Li Ling ◽  
Maria Bacia ◽  
...  
Keyword(s):  
Self Assembly ◽  
Protein Crystallization ◽  
Building Blocks ◽  
Oriented Attachment ◽  
Great Promise ◽  
Inorganic Systems ◽  
Maturation Stages ◽  
Designer Proteins ◽  
Rate Limit ◽  
Classical Mechanism

AbstractSelf-assembly of proteins holds great promise for the bottom-up design and production of synthetic biomaterials. In conventional approaches, designer proteins are pre-programmed with specific recognition sites that drive the association process towards a desired organized state. Although proven effective, this approach poses restrictions on the complexity and material properties of the end-state. An alternative, hierarchical approach that has found wide adoption for inorganic systems, relies on the production of crystalline nanoparticles which in turn become the building blocks of a next-level assembly process driven by oriented attachment (OA). As it stands, OA has not been observed for proteins. Here we employ cryoEM in the high nucleation rate limit of protein crystals and map the self-assembly route at molecular resolution. We observe the initial formation of facetted nanocrystals that merge lattices by means of OA alignment well before contact is made, satisfying non-trivial symmetry rules in the process. The OA mechanism yields crystal morphologies that are not attainable through conventional crystallization routes. Based on these insights we revisit a system of protein crystallization that has long been classified as non-classical, but our data is in direct conflict with that conclusion supporting a classical mechanism that implicates OA. These observations raise further questions about past conclusions for other proteins and illustrate the importance of maturation stages after primary nucleation has taken place.

Designer Proteins

Science ◽  
2003 ◽  
Vol 301 (5635) ◽  
pp. 891m-891
Keyword(s):  
Designer Proteins
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