Biophysical dissection of membrane proteins

By S. White. 2009

285 citations recorded by the source corpus.

The first atomic-resolution structure of a membrane protein was solved in 1985. Twenty-four years and more than 180 unique structures later, what have we have learned? An examination of the atomic details of several diverse membrane proteins reveals some remarkable biophysical features and suggests that we can expect to achieve much more in the decades to come.

Subfields: Molecular Biology

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Citations in the corpus

Structural model of PORCN illuminates disease-associated variants and drug binding sites (2021, unknown): “Here, taking advantage of advances in structural prediction algorithms, we developed a high-quality structural homology model of human PORCN (Sánchez and Šali, 1997; Vyas et al., 2012; White, 2009).”
Accurate de novo structure prediction of large transmembrane protein domains using fragment-assembly and correlated mutation analysis (2012, unknown): “Sab ij 1⁄4 f ðAiBjÞ − f ðAiÞf ðBjÞ; [1]”
Transmembrane Membrane Readers form a Novel Class of Proteins That Include Peripheral Phosphoinositide Recognition Domains and Viral Spikes (2022, methodology): “Membrane protein structures were obtained by surveying the RCSB Protein Data‐ Bank (PDB) [24], Membranome [25], OPM [12], PDBTM [26], MemProtMD [27], and mpstruc [28].”
De Novo Structure Prediction of Globular Proteins Aided by Sequence Variation-Derived Contacts (2014, background): “Although Pfam covers all types of proteins, transmembrane proteins contribute to a negligible fraction of about 3% of all Pfam families (by cross-referencing to UniProt), whereas they constitute about 30% of a typical genome [38].”