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Designed Protein-Protein Association
Science, 2008The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, demonstrating that a given protein can be engineered to form contacts at various points of its surface.
Grueninger, Dirk +5 more
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Designing cooperativity into the designed protein Top7
Proteins: Structure, Function, and Bioinformatics, 2013ABSTRACTThe topology of the designed protein Top7 is not found in natural proteins. Top7 shows signatures of non‐cooperative folding in both experimental studies and computer simulations. In particular, molecular dynamics of coarse‐grained structure‐based models of Top7 show a well‐populated C‐terminal folding‐intermediate.
Shilpa, Yadahalli, Shachi, Gosavi
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Design and designability of protein-based assemblies
Current Opinion in Structural Biology, 2014Design of protein-based assemblies is an exciting frontier in molecular engineering. It can be seen as an extension of the protein design problem, but with some added hurdles. In recent years, much of the focus in the field has been on patterning existing protein structural units (proteins, oligomers, or structural motifs) to design diverse assembly ...
Jian, Zhang +2 more
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Computational Protein Design [PDF]
Nature Reviews Methods PrimersCombining molecular modelling, machine-learned models and an increasingly detailed understanding of protein chemistry and physics, computational protein design and human expertise have been able to produce new protein structures, assemblies and functions that do not exist in nature. Currently, generative deep-learning-based methods, which exploit large
Thomas Schiex +2 more
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Current Opinion in Biotechnology, 1991
Several noteworthy papers have been published in the past year in which the creation of interesting novel proteins, either by de novo design or the redesign of existing proteins, has been reported. Highlights include the successful design of proteins for binding specific ligands.
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Several noteworthy papers have been published in the past year in which the creation of interesting novel proteins, either by de novo design or the redesign of existing proteins, has been reported. Highlights include the successful design of proteins for binding specific ligands.
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Current Opinion in Biotechnology, 1998
It is now possible to design small proteins capable of folding into compact structures with well-packed cores. Given the present state of knowledge of protein folding and design, it is possible to extract a set of engineering guidelines that may assist in future de novo protein design.
C E, Schafmeister, R M, Stroud
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It is now possible to design small proteins capable of folding into compact structures with well-packed cores. Given the present state of knowledge of protein folding and design, it is possible to extract a set of engineering guidelines that may assist in future de novo protein design.
C E, Schafmeister, R M, Stroud
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Bioinformatics and Protein Design
Current Pharmaceutical Biotechnology, 2002Traditionally, the development of drugs has focused on small molecule therapeutics. However, with recent advances in recombinant protein technology the potential of proteins as therapeutics is starting to be realized. Already there are protein drugs on the market, including naturally occurring proteins, engineered proteins and proteins introduced into ...
Roman A, Laskowski, A W Edith, Chan
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Synthetic Proteins: Designer proteins
Current Biology, 1994Attempts to synthesize de novo proteins with particular properties should improve our understanding of the long-range cooperative interactions that are so crucial to the structure and function of proteins.
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Current Opinion in Structural Biology, 2002
Combinatorial protein libraries permit the examination of a wide range of sequences. Such methods are being used for denovo design and to investigate the determinants of protein folding. The exponentially large number of possible sequences, however, necessitates restrictions on the diversity of sequences in a combinatorial library.
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Combinatorial protein libraries permit the examination of a wide range of sequences. Such methods are being used for denovo design and to investigate the determinants of protein folding. The exponentially large number of possible sequences, however, necessitates restrictions on the diversity of sequences in a combinatorial library.
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The designability of protein structures
Journal of Molecular Graphics and Modelling, 2001It has been noted that natural proteins adapt only a limited number of folds. Several researchers have investigated why and how nature has selected this small number of folds. Using simple models of protein folding, we demonstrate systematically that there is a "designability principle" behind nature's selection of protein folds. The designability of a
R, Helling +6 more
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