Analysis of the solution structure of human interleukin-4 determined by heteronuclear three-dimensional nuclear magnetic resonance techniques. by Redfield, C, Smith, L, Boyd, J, Lawrence, G, Edwards, R, Gershater, C, Smith, R, Dobson, C

Studies of protein folding by NMR spectroscopy by Eyles, S

Subjects:

Protein structures from NMR data by Smith, L, Smith, Lorna

Subjects:

Solid state NMR studies of transition metal compounds by Smith, D, Smith, Deborah Jane

Subjects: “…Nuclear magnetic resonance…”

Comparison of four independently determined structures of human recombinant interleukin-4. by Smith, L, Redfield, C, Smith, R, Dobson, C, Clore, G, Gronenborn, A, Walter, MR, Naganbushan, T, Wlodawer, A

“…Four independent structures of human interleukin-4, two determined by nuclear magnetic resonance techniques and two by X-ray diffraction, have been compared in detail. …”

Detection of transient protein folding populations by mass spectrometry. by Miranker, A, Robinson, C, Radford, SE, Aplin, RT, Dobson, C

“…This information is complementary to that from nuclear magnetic resonance spectroscopy (NMR) experiments, which measure the average occupancy of individual sites over the distribution of protein molecules. …”

Long-range interactions within a nonnative protein. by Klein-Seetharaman, J, Oikawa, M, Grimshaw, S, Wirmer, J, Duchardt, E, Ueda, T, Imoto, T, Smith, L, Dobson, C, Schwalbe, H

“…We have used a combination of nuclear magnetic resonance (NMR) spectroscopy and site-directed mutagenesis to study unfolded states of the protein lysozyme. …”

Human interleukin 4. The solution structure of a four-helix bundle protein. by Smith, L, Redfield, C, Boyd, J, Lawrence, G, Edwards, R, Smith, R, Dobson, C

“…Heteronuclear 13C and 15N three-dimensional nuclear magnetic resonance (n.m.r.) techniques have been used to determine the solution structure of human interleukin 4, a four-helix bundle protein. …”

Probing the exposure of tyrosine and tryptophan residues in partially folded proteins and folding intermediates by CIDNP pulse-labeling. by Lyon, C, Suh, E, Dobson, C, Hore, P

“…A nuclear magnetic resonance (NMR) technique has been devised to probe the structures of disordered, partially folded states of proteins at the level of individual amino acid residues. …”

The conformation of lysozyme in solution by Dobson, C, Dobson, Christopher Martin

“…<p>This thesis describes an investigation of the conformation of a small protein, lysozyme from hen egg-white, in aqueous solution which was carried out by means of nuclear magnetic resonance (nmr) spectroscopy. The conformation in the crystalline state had previously been investigated by X-ray diffraction, and a model of this conformation (the X-ray structure) was available. …”

Molecular recycling within amyloid fibrils. by Carulla, N, Caddy, G, Hall, DR, Zurdo, J, Gairí, M, Feliz, M, Giralt, E, Robinson, C, Dobson, C

“…Here we have probed the nature of the amyloid structure by monitoring hydrogen/deuterium exchange in fibrils formed from an SH3 domain using a combination of nuclear magnetic resonance spectroscopy and electrospray ionization mass spectrometry. …”

Structure of hen lysozyme in solution. by Smith, L, Sutcliffe, M, Redfield, C, Dobson, C

“…The structure of the 129-residue protein hen lysozyme has been determined in solution by two-dimensional 1H nuclear magnetic resonance methods. 1158 NOE distance restraints, and 68 phi and 24 chi 1 dihedral angle restraints were employed in conjunction with distance geometry and simulated annealing procedures. …”

Exploration of partially unfolded states of human alpha-lactalbumin by molecular dynamics simulation. by Paci, E, Smith, L, Dobson, C, Karplus, M

“…The resulting structures are relaxed by unbiased simulations and used as models of the molten globule and partly denatured states of human alpha-LA, based on measured radii of gyration obtained from nuclear magnetic resonance experiments. The ensembles of structures agree in their overall properties with experimental data available for the human alpha-LA molten globule and its more denatured states. …”

Rapid sample-mixing technique for transient NMR and photo-CIDNP spectroscopy: applications to real-time protein folding. by Mok, K, Nagashima, T, Day, I, Jones, J, Jones, C, Dobson, C, Hore, P

“…We describe the development and application of a novel rapid sample-mixing technique for real-time NMR (nuclear magnetic resonance) spectroscopy. The apparatus consists of an insert inside a conventional NMR tube coupled to a rapid injection syringe outside the NMR magnet. …”

NMR studies of the dynamics and the folding of hen lysozyme by Buck, M, Buck, Matthias

“…The native state, a partially structured state generated by the addition of a cosolvent, trifluoroethanol (TFE), and a highly denatured state of the protein in presence of urea at low pH, have been studied at equilibrium by circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy. The principal methods utilised in-fchis thesis are the measurement and interpretation of amide hydrogen exchange and ¹⁵ N relaxation data.…”