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15 papers found.
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Outer membrane protein folding from an energy landscape perspective

The cell envelope is essential for the survival of Gram-negative bacteria. This specialised membrane is densely packed with outer membrane proteins (OMPs), which perform a variety of functions. How OMPs fold into this crowded environment remains an open question. Here, we review current knowledge about OMP folding mechanisms in vitro and discuss how the need to fold to a stable...

Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation

Molecular and Cellular Biology, University of Leeds , Leeds LS2 9JT , UK 1 Sheena E. Radford Aggregation of the amyloid-β (Aβ) peptide is strongly correlated with Alzheimer's disease (AD). Recent research ... /K015958/1) and The Wellcome Trust (089311/ Z/09/Z) for funding. Compliance with ethical standards Conflicts of interest Katie L. Stewart declares that she has no conflicts of interest. Sheena E. Radford

MpUL-multi: Software for Calculation of Amyloid Fibril Mass per Unit Length from TB-TEM Images

Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, University of Leeds, Leeds, LS2 9JT. UKMatthew G. Iadanza, Matthew P. Jackson, Sheena E. Radford & Neil A. Ranson ... AuthorsSearch for Matthew G. Iadanza in:Nature Research journals • PubMed • Google ScholarSearch for Matthew P. Jackson in:Nature Research journals • PubMed • Google ScholarSearch for Sheena E. Radford in:Nature

FPOP-LC-MS/MS Suggests Differences in Interaction Sites of Amphipols and Detergents with Outer Membrane Proteins

Amphipols are a class of novel surfactants that are capable of stabilizing the native state of membrane proteins. They have been shown to be highly effective, in some cases more so than detergent micelles, at maintaining the structural integrity of membrane proteins in solution, and have shown promise as vehicles for delivering native membrane proteins into the gas phase for...

Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS

Collision cross-section (CCS) measurements obtained from ion mobility spectrometry-mass spectrometry (IMS-MS) analyses often provide useful information concerning a protein’s size and shape and can be complemented by modeling procedures. However, there have been some concerns about the extent to which certain proteins maintain a native-like conformation during the gas-phase...

Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM

Preston Street, Leeds LS2 9JT, UKMatthew G. Iadanza, Anna J. Higgins, Bob Schiffrin, Antonio N. Calabrese, David J. Brockwell, Alison E. Ashcroft, Sheena E. Radford & Neil A. Ranson AuthorsSearch for ... Alison E. Ashcroft in:Nature Research journals • PubMed • Google ScholarSearch for Sheena E. Radford in:Nature Research journals • PubMed • Google ScholarSearch for Neil A. Ranson in:Nature Research

Dissecting key residues in folding and stability of the bacterial immunity protein 7

The small four-helix immunity protein, Im7, has previously been shown to fold via a compact intermediate containing three of the four native helices. The short, six-residue helix III only docks onto the developing Im7 structure after the rate-limiting second transition state has been traversed. Previous work demonstrated that mutation of the helix III sequence can be used to trap...

β2-Microglobulin Amyloid Fibril-Induced Membrane Disruption Is Enhanced by Endosomal Lipids and Acidic pH

Although the molecular mechanisms underlying the pathology of amyloidoses are not well understood, the interaction between amyloid proteins and cell membranes is thought to play a role in several amyloid diseases. Amyloid fibrils of β2-microglobulin (β2m), associated with dialysis-related amyloidosis (DRA), have been shown to cause disruption of anionic lipid bilayers in vitro...

HDX-ESI-MS reveals enhanced conformational dynamics of the amyloidogenic protein β 2-microglobulin upon release from the MHC-1

The light chain of the major histocompatibility complex class 1 (MHC-1), the protein β 2-microglobulin (β 2m), has amyloidogenic properties that arise only upon its dissociation from the MHC-1. Here hydrogen/deuterium exchange electrospray ionization mass spectrometry (HDX-ESI-MS) has been used to compare the solution dynamics of β 2m in its MHC-1 bound state compared with those...

Characterization of the Response of Primary Cells Relevant to Dialysis-Related Amyloidosis to β2-Microglobulin Monomer and Fibrils

The formation of insoluble amyloid fibrils is associated with an array of devastating human diseases. Dialysis-related amyloidosis (DRA) is a severe complication of hemodialysis that results in the progressive destruction of the bones and joints. Elevated concentrations of β2-microglobulin (β2m) in the serum of subjects on hemodialysis promote the formation of amyloid fibrils in...

A Force-Activated Trip Switch Triggers Rapid Dissociation of a Colicin from Its Immunity Protein

. Radford 0 David J. Brockwell 0 Wendy E. Thomas, University of Washington, United States of America 0 1 School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, United

Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis

Wei-Feng Xue 0 Steve W. Homans 0 Sheena E. Radford 0 0 Astbury Centre for Structural Molecular Biology, Institute of Molecular and Cellular Biology, University of Leeds , Leeds LS2 9JT, UK 1To whom

Second Order Rate Constants of Donor-Strand Exchange Reveal Individual Amino Acid Residues Important in Determining the Subunit Specificity of Pilus Biogenesis

P pili are hair-like adhesive structures that are assembled on the outer membrane (OM) of uropathogenic Escherichia coli by the chaperone-usher pathway. In this pathway, chaperone-subunit complexes are formed in the periplasm and targeted to an OM assembly platform, the usher. Pilus subunits display a large groove caused by a missing β-strand which, in the chaperone-subunit...

Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry

The precise mechanism of protein folding remains elusive and there is a deficiency of biophysical techniques that are capable of monitoring the individual behavior of copopulated protein conformers during the folding process. Herein, an ion mobility spectrometry (IMS) device integrated with electrospray ionization mass spectrometry (ESI-MS) has been used to successfully separate...

Helix stability and hydrophobicity in the folding mechanism of the bacterial immunity protein Im9

Recent models suggest that the mechanism of protein folding is determined by the balance between the stability of secondary structural elements and the hydrophobicity of the sequence. Here we determine the role of these factors in the folding kinetics of Im9* by altering the secondary structure propensity or hydrophobicity of helices I, II or IV by the substitution of residues at...