Fluorescent proteins and genetically encoded biosensors

M Wang, Y Da, Y Tian - Chemical Society Reviews, 2023 - pubs.rsc.org
The genetically encoded fluorescent sensors convert chemical and physical signals into
light. They are powerful tools for the visualisation of physiological processes in living cells …

Aromatic-aromatic interaction: a mechanism of protein structure stabilization

SK Burley, GA Petsko - Science, 1985 - science.org
Analysis of neighboring aromatic groups in four biphenyl peptides or peptide analogs and
34 proteins reveals a specific aromatic-aromatic interaction. Aromatic pairs (< 7 Å between …

Nanopore-based measurements of protein size, fluctuations, and conformational changes

P Waduge, R Hu, P Bandarkar, H Yamazaki… - ACS …, 2017 - ACS Publications
Proteins are structurally dynamic macromolecules, and it is challenging to quantify the
conformational properties of their native state in solution. Nanopores can be efficient tools to …

Three-dimensional structure of myosin subfragment-1: a molecular motor

I Rayment, WR Rypniewski, K Schmidt-Bäse, R Smith… - Science, 1993 - science.org
Directed movement is a characteristic of many living organisms and occurs as a result of the
transformation of chemical energy into mechanical energy. Myosin is one of three families of …

Structural analysis of substrate binding by the molecular chaperone DnaK

X Zhu, X Zhao, WF Burkholder, A Gragerov, CM Ogata… - Science, 1996 - science.org
DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote
protein folding, interaction, and translocation, both constitutively and in response to stress …

Structures and metal-ion-binding properties of the Ca2+-binding helix–loop–helix EF-hand motifs

JL Gifford, MP Walsh, HJ Vogel - Biochemical Journal, 2007 - portlandpress.com
The 'EF-hand'Ca2+-binding motif plays an essential role in eukaryotic cellular signalling,
and the proteins containing this motif constitute a large and functionally diverse family. The …

Modulation of cardiac ryanodine receptor 2 by calmodulin

D Gong, X Chi, J Wei, G Zhou, G Huang, L Zhang… - Nature, 2019 - nature.com
The high-conductance intracellular calcium (Ca2+) channel RyR2 is essential for the
coupling of excitation and contraction in cardiac muscle. Among various modulators …

Structure of calmodulin refined at 2.2 Å resolution

YS Babu, CE Bugg, WJ Cook - Journal of molecular biology, 1988 - Elsevier
The crystal structure of mammalian calmodulin has been refined at 2.2 Å (1 Å= 0.1 nm)
resolution using a restrained least-squares method. The final crystallographic R-factor …

Structural diversity of calmodulin binding to its target sites

H Tidow, P Nissen - The FEBS journal, 2013 - Wiley Online Library
Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and
regulates a number of diverse target proteins involved in different functions such as …

Solution structure of a calmodulin-target peptide complex by multidimensional NMR

M Ikura, GM Clore, AM Gronenborn, G Zhu, CB Klee… - Science, 1992 - science.org
The three-dimensional solution structure of the complex between calcium-bound calmodulin
(Ca2+-CaM) and a 26-residue synthetic peptide comprising the CaM binding domain …