Search Results

You searched for all publications:

with publication states 'Published (Approved)'

Search Again...

These results only include publications that have been reviewed and processed by Diamond Light Source. To also view papers that have not yet been processed click here.

You can use the folder icon under Actions to collate papers as required. You can then click on View Folder in the left-hand navigation to review and/or download your folder.

Exact matches
Related results

107 items found (0 items not approved), displaying 11 to 20.[First/Prev] 1, 2, 3, 4, 5, 6, 7, 8 [Next/Last]

Instruments / Technical Area	Publication Details	Published
B23-Circular Dichroism	Update on Diamond SRCD beamline B23 Tamas Javorfi , Rohanah Hussain , Giuliano Siligardi 2nd International Workshop on Synchrotron Radiation Circular Dichroism Spectroscopy	Apr 2009
	Ligand interactions: Challenges ahead using SRCD Rohanah Hussain , Guiliano Siligardi 2nd International Workshop on Synchrotron Radiation Circular Dichroism Spectroscopy	Apr 2009
	A Proposed New Light Source Facility for the UK R. P. Walker , R. Bartolini , C. Christou , J-h. Han , J. Kay , G. Rehm , J. Rowland , D. Angal-kalinin , J. A. Clarke , D. J. Dunning , A. R. Goulden , F. Jackson , S. P. Jamison , J. K. Jones , K. B. Marinov , P. A. Mcintosh , J. Mckenzie , B. L. Militsyn , A. J. Moss , I. P. Martin Particle Accelerator Conference 2009 (Vancouver) Show Abstract ▼ Abstract: The New Light Source (NLS) project was launched in April 2008 by the UK Science and Technology Facilities Council (STFC) to consider the scientific case and develop a conceptual design for a possible next generation light source based on a combination of advanced conventional laser and free-electron laser sources. Following a series of workshops and a period of scientific consultation, the science case was approved in October 2008 and the go-ahead given to continue the project to the design stage. In November the decision was taken that the facility will be based on cw superconducting technology in order to provide the best match to the scientific objectives. In this paper we present the source requirements, both for baseline operation and with possible upgrades, and the current status of the design of the accelerator driver and free-electron laser sources to meet those requirements.	May 2009
	A novel drug delivery approach for the formulation of lipophilic therapeutics of small molecule peptide-based and protein drugs Rohanah Hussain , Giuliano Siligardi 12th International Conference on Circular Dichroism	Aug 2009
	A novel cationic lipopeptide therapeutics with a broad range of antimicrobial activites Rohanah Hussain , Giuliano Siligardi 12th International Conference on Circular Dichroism	Aug 2009
B23-Circular Dichroism	Overview of ligand interactions using circular dichroism Guiliano Siligardi , Rohanah Hussain 12th International Conference on Circular Dichroism	Aug 2009
B23-Circular Dichroism	Circular Dichroism Beamline at Diamond Light Source Tamas Javorfi , Rohanah Hussain , Daniel Myatt , Guiliano Siligardi 12th International Conference on Circular Dichroism	Aug 2009
B23-Circular Dichroism	Recognition of lysine-rich peptideligands by murine cortactin SH3 domain: CD, ITC and NMR studies Chiara Rubini , Paolo Ruzza , Mark R. Spaller , D. Gomika Udugamasooriya , Massimo Ballanda , Steafno Mammi , Andrea Borgogno , Andrea Calderan , Luca Cesaro , Anna M. Brunati , Arianna Donella-deana , Rohanah Hussain , Giuliano Siligardi Biopolymers DOI: 10.1002/bip.21350 Show Abstract ▼ Abstract: Cortactin is a ubiquitous actin-binding protein that regulates various aspects of cell dynamics and is implicated in the pathogenesis of human neoplasia. The sequence of cortactin contains a number of signaling motifs and an SH3 domain at the C-terminus, which mediates the interaction of the protein with several partners, including Shank2. A recombinant protein, comprising the murine cortactin SH3 domain fused to GST (GST-SH3(m-cort)), was prepared and used to assess the domain-binding affinity of potential peptide-ligands reproducing the proline-rich regions of human HPK1 and Shank2 proteins. The key residues involved in the SH3(m-cort) domain recognition were identified by three different approaches: non-immobilized ligand interaction assay by circular dichroism, isothermal titration calorimetry and nuclear magnetic resonance. Our results show that the classical PxxPxK class II binding motif is not sufficient to mediate the interaction with GST-SH3(m-cort), an event that depends on the presence of additional basic residues located at either the N- or the C-terminus of the PxxPxK motif Especially effective in promoting the peptide binding is a Lys residue at the -5 position, a determinant present in both P2 (HPK1 394403) and S1 (Shank2 1168-1189) peptides. GST-SH3(m-cort) exhibits the highest affinity toward peptide Si, which contains additional Lys residues at the -3, -5, and -7 positions, indicating that the optimal consensus motif may be KPPxPxKxKxK. These results are supported by the in silico models of SH3(m-cort) complexed with P2 or S1, which highlight the domain residues that interact with the recognition determinants of the peptide-ligand and cooperate in binding stabilization. (C) 2009 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 94: 298-306, 2010.	Nov 2009
B23-Circular Dichroism	Raman and Raman optical activity of glycosaminoglycans Timothy Rudd , Rohanah Hussain , Guiliano Siligardi , Edwin Yates Chemical Communications 46 (23), 4124-4126 DOI: 10.1039/c001535k Diamond Proposal Number(s): [1559] Show Abstract ▼ Abstract: The first Raman optical activity spectra of glycosaminoglycans (GAGs) are reported and exhibited characteristic features specific to the major chemical differences in GAGs (N-, O-sulfation and N-acetylation). Furthermore, the lack of major features between 1050-1150 cm(-1) for heparin and N-acetyl heparin suggests that these molecules do not adopt strongly helical conformations in solution and indicate subtly different solution conformations.	Jan 2010
	Applications of Circular Dichroism Giuliano Siligardi , Rohanah Hussain DOI: 10.1016/B978-0-12-374413-5.00031-2 Show Abstract ▼ Abstract: Circular dichroism (CD) spectroscopy is the technique of choice to study chiral molecules in solution, in particular biologically important molecules such as proteins, nucleic acids, carbohydrates, and therapeutic drugs. An important application of CD spectroscopy is the determination of the equilibrium dissociation constant, Kd, of binding interactions between a macromolecular host and a ligand. The Kd can be calculated by analyzing CD data at fixed wavelength versus ligand concentration using a nonlinear regression method. Several examples of CD titrations are illustrated here to describe the ‘golden’ rules on how to determine the molecular binding interactions of nonimmobilized and nonlabeled systems of biologically important molecules by CD spectroscopy.	Jan 2010

Publications Database

Search Results

You searched for all publications:

Search Again...

Subject Areas (check all that apply) select all

Instruments used to collect data (check all that apply) select all

Collaborations involved (check all that apply) select all

Diamond Offline Facilities used

Relevant Technical Areas (check all that apply) select all

Menu for Anonymous User