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Current Opinion in Biotechnology, ISSN 0958-1669, 08/2019, Volume 58, p. 175
Journal Article
ACS Chemical Biology, ISSN 1554-8929, 02/2017, Volume 12, Issue 2, pp. 528 - 538
Journal Article
Nature Chemical Biology, ISSN 1552-4450, 08/2010, Volume 6, Issue 8, pp. 615 - 620
Hydrogen bonds between backbone amides are common in folded proteins. Here, we show that an intimate interaction between backbone amides likewise arises from... 
Journal Article
Current Opinion in Biotechnology, ISSN 0958-1669, 08/2019, Volume 58, pp. 175 - 182
One approach to designing proteinaceous assemblies and materials is to develop simple, standardised building blocks and then to combine these symmetrically to... 
IN-VITRO | SYMMETRY | EVOLUTION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | COMPUTATIONAL DESIGN | BIOCHEMICAL RESEARCH METHODS | NANOMATERIALS | NANOTUBES | CAGES | NANOSTRUCTURES | COILED COILS | PROTEIN NANOPARTICLES
Journal Article
Science, ISSN 0036-8075, 07/2017, Volume 357, Issue 6347, pp. 133 - 134
How does the amino acid sequence of a protein chain determine and maintain its three-dimensional folded state? Answering this question--a key aspect of the... 
PROTEIN DESIGN | STABILITY | MULTIDISCIPLINARY SCIENCES | Models, Molecular | Amino Acid Sequence | Protein Conformation | Proteins | Design | Protein folding | Amino acid sequence | Protein structure | Folding | Structure-function relationships
Journal Article
Current Opinion in Chemical Biology, ISSN 1367-5931, 10/2019, Volume 52, pp. 102 - 111
Our ability to design completely proteins is improving rapidly. This is true of all three main approaches to protein design, which we define as: minimal,... 
Journal Article
NATURE CHEMICAL BIOLOGY, ISSN 1552-4450, 08/2010, Volume 6, Issue 8, pp. 615 - 620
Hydrogen bonds between backbone amides are common in folded proteins. Here, we show that an intimate interaction between backbone amides also arises from the... 
ALPHA-HELIX | THERMODYNAMICS | MECHANISM | MOLECULE | STABILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | RESOLUTION | SECONDARY STRUCTURE | CONFORMATION | ENERGIES | PROLINE | Hydrogen Bonding | Protein Structure, Secondary | Computational Biology | Models, Molecular | Crystallography, X-Ray | Protein Conformation | Proteins - chemistry | Dipeptides - chemistry | Databases, Nucleic Acid
Journal Article
Bioinformatics, ISSN 1367-4803, 10/2018, Volume 34, Issue 19, pp. 3316 - 3323
Abstract Motivation To understand protein structure, folding and function fully and to design proteins de novo reliably, we must learn from natural protein... 
VIRUS | BIOCHEMICAL RESEARCH METHODS | ENVELOPE GLYCOPROTEIN | PERIODIC-TABLE | MEMBRANE-PROTEIN | ALPHA-HELICAL BARRELS | DE-NOVO DESIGN | ASSEMBLIES | DATABASE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | MATHEMATICAL & COMPUTATIONAL BIOLOGY | CORE STRUCTURE | CORONAVIRUS SPIKE PROTEIN | Original Papers
Journal Article
Protein Science, ISSN 0961-8368, 03/2014, Volume 23, Issue 3, p. 284
  The folding of proteins is directed by a variety of interactions, including hydrogen bonding, electrostatics, van der Waals' interactions, and the... 
Plasma | Protein folding
Journal Article
Protein Science, ISSN 0961-8368, 04/2016, Volume 25, Issue 4, pp. 887 - 897
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 12/2013, Volume 135, Issue 49, pp. 18682 - 18688
Protein structures are stabilized by multiple weak interactions, including the hydrophobic effect, hydrogen bonds, electrostatic effects, and van der Waals... 
Proteins - chemistry | Hydrogen Bonding | Static Electricity | Asparagine - chemistry
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 06/2019, Volume 141, Issue 22, pp. 8787 - 8797
The association of amphipathic α helices in water leads to α-helical-bundle protein structures. However, the driving force for this-the hydrophobic effect-is... 
Journal Article
Nature Chemistry, ISSN 1755-4330, 05/2017, Volume 9, Issue 5, p. 411
  The fabrication of monodisperse transmembrane barrels formed from short synthetic peptides has not been demonstrated previously. This is in part because of... 
Journal Article
ISSN 2041-6520, 10/2018, Volume 9, Issue 39, pp. 7656 - 7665
Protein-protein interactions (PPIs) play pivotal roles in the majority of biological processes. Therefore, improved approaches to target and disrupt PPIs would... 
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 08/2017, Volume 114, Issue 34, p. 9014
The formation of quasi-spherical cages from protein building blocks is a remarkable self-assembly process in many natural systems, where a small number of... 
Self assembly | Shells | Cages | Icosahedral phase | Design optimization | Studies | Proteins | Self-assembly | Packing | Control surfaces | Surface properties | Spherical shells | Symmetry
Journal Article
Protein Science, ISSN 0961-8368, 03/2014, Volume 23, Issue 3, pp. 284 - 288
Journal Article
Chemical Society Reviews, ISSN 0306-0012, 09/2010, Volume 39, Issue 9, pp. 3464 - 3479
Journal Article
Chemical Science, ISSN 2041-6520, 01/2018, Volume 9, Issue 39, pp. 7656 - 7665
Protein–protein interactions (PPIs) play pivotal roles in the majority of biological processes. Therefore, improved approaches to target and disrupt PPIs would... 
Proteins | Coils | Organic chemistry | Residues | Alanine | Inhibitors | Peptides | Coiling | Dependence | Disruption | Biological activity
Journal Article
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