Rotational Resonance NMR Structural Studies of the Neu Receptor Transmembrane Domain.

1995 ◽  
Author(s):  
Steven O. Smith
Keyword(s):  
Transmembrane Domain ◽  
Structural Studies ◽  
Rotational Resonance

scholarly journals Conformational rearrangements in the transmembrane domain of CNGA1 channels revealed by single-molecule force spectroscopy

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Sourav Maity ◽  
Monica Mazzolini ◽  
Manuel Arcangeletti ◽  
Alejandro Valbuena ◽  
Paolo Fabris ◽  
...  
Keyword(s):  
Single Molecule ◽  
Conformational Changes ◽  
Transmembrane Domain ◽  
Force Spectroscopy ◽  
Dynamic Structure ◽  
Transmembrane Domains ◽  
Structural Studies ◽  
Single Molecule Force Spectroscopy ◽  
Conformational Rearrangements ◽  
Α Helix

Abstract Cyclic nucleotide-gated (CNG) channels are activated by binding of cyclic nucleotides. Although structural studies have identified the channel pore and selectivity filter, conformation changes associated with gating remain poorly understood. Here we combine single-molecule force spectroscopy (SMFS) with mutagenesis, bioinformatics and electrophysiology to study conformational changes associated with gating. By expressing functional channels with SMFS fingerprints in Xenopus laevis oocytes, we were able to investigate gating of CNGA1 in a physiological-like membrane. Force spectra determined that the S4 transmembrane domain is mechanically coupled to S5 in the open state, but S3 in the closed state. We also show there are multiple pathways for the unfolding of the transmembrane domains, probably caused by a different degree of α-helix folding. This approach demonstrates that CNG transmembrane domains have dynamic structure and establishes SMFS as a tool for probing conformational change in ion channels.

scholarly journals Structural Studies Providing Insights into Production and Conformational Behavior of Amyloid-β Peptide Associated with Alzheimer’s Disease Development

Molecules ◽  
2021 ◽  
Vol 26 (10) ◽  
pp. 2897
Author(s):  
Anatoly S. Urban ◽  
Konstantin V. Pavlov ◽  
Anna V. Kamynina ◽  
Ivan S. Okhrimenko ◽  
Alexander S. Arseniev ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Molecular Mechanisms ◽  
Transmembrane Domain ◽  
Senile Plaques ◽  
Amyloid Β ◽  
Conformational Behavior ◽  
Amyloid Β Peptide ◽  
Structural Studies ◽  
Aβ Production

Alzheimer’s disease is the most common type of neurodegenerative disease in the world. Genetic evidence strongly suggests that aberrant generation, aggregation, and/or clearance of neurotoxic amyloid-β peptides (Aβ) triggers the disease. Aβ accumulates at the points of contact of neurons in ordered cords and fibrils, forming the so-called senile plaques. Aβ isoforms of different lengths are found in healthy human brains regardless of age and appear to play a role in signaling pathways in the brain and to have neuroprotective properties at low concentrations. In recent years, different substances have been developed targeting Aβ production, aggregation, interaction with other molecules, and clearance, including peptide-based drugs. Aβ is a product of sequential cleavage of the membrane glycoprotein APP (amyloid precursor protein) by β- and γ-secretases. A number of familial mutations causing an early onset of the disease have been identified in the APP, especially in its transmembrane domain. The mutations are reported to influence the production, oligomerization, and conformational behavior of Aβ peptides. This review highlights the results of structural studies of the main proteins involved in Alzheimer’s disease pathogenesis and the molecular mechanisms by which perspective therapeutic substances can affect Aβ production and nucleation.

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

Sign in / Sign up

Export Citation Format

Share Document