Structure, dynamics, assembly, and evolution of protein complexes
JA Marsh, SA Teichmann - Annual review of biochemistry, 2015 - annualreviews.org
The assembly of individual proteins into functional complexes is fundamental to nearly all
biological processes. In recent decades, many thousands of homomeric and heteromeric …
biological processes. In recent decades, many thousands of homomeric and heteromeric …
Residue mutations and their impact on protein structure and function: detecting beneficial and pathogenic changes
The present review focuses on the evolution of proteins and the impact of amino acid
mutations on function from a structural perspective. Proteins evolve under the law of natural …
mutations on function from a structural perspective. Proteins evolve under the law of natural …
Structure–function relationship of terpenoid glycosyltransferases from plants
E Kurze, M Wüst, J Liao, K McGraphery… - Natural Product …, 2022 - pubs.rsc.org
Covering: up to 2021 Terpenoids are physiologically active substances that are of great
importance to humans. Their physicochemical properties are modified by glycosylation, in …
importance to humans. Their physicochemical properties are modified by glycosylation, in …
Trigger factor both holds and folds its client proteins
ATP-independent chaperones like trigger factor are generally assumed to play passive roles
in protein folding by acting as holding chaperones. Here we show that trigger factor plays a …
in protein folding by acting as holding chaperones. Here we show that trigger factor plays a …
Insertions and deletions (indels): a missing piece of the protein engineering jigsaw
CM Miton, N Tokuriki - Biochemistry, 2022 - ACS Publications
Over the years, protein engineers have studied nature and borrowed its tricks to accelerate
protein evolution in the test tube. While there have been considerable advances, our ability …
protein evolution in the test tube. While there have been considerable advances, our ability …
Structural, evolutionary, and assembly principles of protein oligomerization
ED Levy, SA Teichmann - Progress in molecular biology and translational …, 2013 - Elsevier
Abstract In the protein universe, 30–50% of proteins self-assemble to form symmetrical
complexes consisting of multiple copies of themselves, called homomers. The prevalence of …
complexes consisting of multiple copies of themselves, called homomers. The prevalence of …
Protein oligomer engineering: a new frontier for studying protein structure, function, and toxicity
C Liu, J Luo - Angewandte Chemie, 2023 - Wiley Online Library
Prevalent in nature, protein oligomers play critical roles both physiologically and
pathologically. The multimeric nature and conformational transiency of protein oligomers …
pathologically. The multimeric nature and conformational transiency of protein oligomers …
Accessing unexplored regions of sequence space in directed enzyme evolution via insertion/deletion mutagenesis
Insertions and deletions (InDels) are frequently observed in natural protein evolution, yet
their potential remains untapped in laboratory evolution. Here we introduce a transposon …
their potential remains untapped in laboratory evolution. Here we introduce a transposon …
[HTML][HTML] How gene duplication diversifies the landscape of protein oligomeric state and function
Oligomeric proteins are central to cellular life and the duplication and divergence of their
genes is a key driver of evolutionary innovations. The duplication of a gene coding for an …
genes is a key driver of evolutionary innovations. The duplication of a gene coding for an …
Structural plasticity enables evolution and innovation of RuBisCO assemblies
Oligomerization is a core structural feature that defines the form and function of many
proteins. Most proteins form molecular complexes; however, there remains a dearth of …
proteins. Most proteins form molecular complexes; however, there remains a dearth of …