Journal ArticleDOI
NMR of membrane-associated peptides and proteins.
TLDR
Recent advances in solution NMR allowing the study of a select set of peripheral and integral membrane proteins, including surface-binding proteins, transmembrane proteins including bacterial outer membrane beta-barrel proteins and oligomeric alpha-helical proteins are described.Abstract:
In living cells, membrane proteins are essential to signal transduction, nutrient use, and energy exchange between the cell and environment. Due to challenges in protein expression, purification and crystallization, deposition of membrane protein structures in the Protein Data Bank lags far behind existing structures for soluble proteins. This review describes recent advances in solution NMR allowing the study of a select set of peripheral and integral membrane proteins. Surface-binding proteins discussed include amphitropic proteins, antimicrobial and anticancer peptides, the HIV-1 gp41 peptides, human alpha-synuclein and apolipoproteins. Also discussed are transmembrane proteins including bacterial outer membrane beta-barrel proteins and oligomeric alpha-helical proteins. These structural studies are possible due to solubilization of the proteins in membrane-mimetic constructs such as detergent micelles and bicelles. In addition to protein dynamics, protein-lipid interactions such as those between arginines and phosphatidylglycerols have been detected directly by NMR. These examples illustrate the unique role solution NMR spectroscopy plays in structural biology of membrane proteins.read more
Citations
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The glycosylphosphatidylinositol anchor: a complex membrane-anchoring structure for proteins.
TL;DR: The structural diversity of the GPI anchor and its putative cellular functions, including involvement in lipid raft partitioning, signal transduction, targeting to the apical membrane, and prion disease pathogenesis are discussed.
Journal ArticleDOI
Human Antimicrobial Peptides and Proteins
TL;DR: It appears that granulysin enters cells and kills intracellular pathogens with the aid of pore-forming perforin, opening new avenues to the development of anti-infectious drugs.
Journal ArticleDOI
Structures of Human Host Defense Cathelicidin LL-37 and Its Smallest Antimicrobial Peptide KR-12 in Lipid Micelles
TL;DR: The structure of LL-37 serves as a model for understanding the structure and function relationship of homologous primate cathelicidins and the smallest antibacterial peptide KR-12, which displayed a selective toxic effect on bacteria but not human cells was identified.
Journal ArticleDOI
The magic of bicelles lights up membrane protein structure.
TL;DR: Recent advances in the field of protein structural biology that have been made possible by exploiting the unique properties of lipid bicelles, in both solution and solid-state NMR spectroscopy, will be discussed.
Journal ArticleDOI
Biophysics of α-Synuclein Membrane Interactions
TL;DR: In this paper, the authors summarize useful biophysical techniques for the study of peripheral membrane proteins and their application in the characterization of the membrane interactions of the natively unfolded and Parkinson's disease related protein, α-synuclein (α-syn) related protein.
References
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Book
NMR of proteins and nucleic acids
TL;DR: The NMR Assignment Problem in Biopolymers, two-Dimensional NMR With Proteins and Nucleic Acids, and Sequence-Specific Resonance Assignments.
Journal ArticleDOI
How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria
TL;DR: The known protein phosphorylation-related regulatory functions of the PTS are summarized, which shows that the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.
Journal ArticleDOI
Anticancer α-Helical Peptides and Structure / Function Relationships Underpinning Their Interactions with Tumour Cell Membranes
TL;DR: It is concluded that alpha-ACPs are major contenders in the search for new anticancer drugs, underlined by the fact that a number of these peptides have been patented in this capacity.