The conformation of lysozyme in solution

The conformation of lysozyme in solution

<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-r...

Cur síos iomlán

Sonraí bibleagrafaíochta
Príomhchruthaitheoirí:	Dobson, C, Dobson, Christopher Martin
Formáid:	Tráchtas
Teanga:	English
Foilsithe / Cruthaithe:	1975

Míreanna comhchosúla

Conformational dynamics and protein unfolding in lysozyme amyloidosis
de réir: Sunde, M, et al.
Foilsithe / Cruthaithe: (1999)

Structure of hen lysozyme in solution.
de réir: Smith, L, et al.
Foilsithe / Cruthaithe: (1993)

Conformational fluctuations of hen lysozyme investigated by high pressure NMR spectroscopy
de réir: Kamatari, Y, et al.
Foilsithe / Cruthaithe: (2003)

Molecular dynamics simulations of peptide fragments from hen lysozyme: insight into non-native protein conformations.
de réir: Smith, L, et al.
Foilsithe / Cruthaithe: (1998)

Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.
de réir: Johnson, R, et al.
Foilsithe / Cruthaithe: (2005)

Oxidative refolding of amyloidogenic variants of human lysozyme.
de réir: Wain, R, et al.
Foilsithe / Cruthaithe: (2005)

Insight into a random coil conformation and an isolated helix: structural and dynamical characterisation of the C-helix peptide from hen lysozyme.
de réir: Bolin, K, et al.
Foilsithe / Cruthaithe: (1996)

Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme.
de réir: Eyles, S, et al.
Foilsithe / Cruthaithe: (1994)

Characterisation of the dominant oxidative folding intermediate of hen lysozyme.
de réir: van den Berg, B, et al.
Foilsithe / Cruthaithe: (1999)

A refined solution structure of hen lysozyme determined using residual dipolar coupling data.
de réir: Schwalbe, H, et al.
Foilsithe / Cruthaithe: (2001)

Side-chain conformations in an unfolded protein: chi1 distributions in denatured hen lysozyme determined by heteronuclear 13C, 15N NMR spectroscopy.
de réir: Hennig, M, et al.
Foilsithe / Cruthaithe: (1999)

Analysis of phi and chi 1 torsion angles for hen lysozyme in solution from 1H NMR spin-spin coupling constants.
de réir: Smith, L, et al.
Foilsithe / Cruthaithe: (1991)

The origin of the alpha-domain intermediate in the folding of hen lysozyme.
de réir: Matagne, A, et al.
Foilsithe / Cruthaithe: (1998)

The solution dynamics of amyloidogenic Asp67His variant of human lysozyme: Insights from hydrogen exchange
de réir: Canet, D, et al.
Foilsithe / Cruthaithe: (2000)

Independent nucleation and heterogeneous assembly of structure during folding of equine lysozyme.
de réir: Morozova-Roche, L, et al.
Foilsithe / Cruthaithe: (1999)

Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy.
de réir: Chamberlain, A, et al.
Foilsithe / Cruthaithe: (2001)

BIOT 243-Biophysical study of the aggregation of human lysozyme into amyloid fibrils
de réir: Dhulesia, A, et al.
Foilsithe / Cruthaithe: (2008)

The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase.
de réir: van den Berg, B, et al.
Foilsithe / Cruthaithe: (1999)

A photochemically induced dynamic nuclear polarization study of denatured states of lysozyme.
de réir: Broadhurst, R, et al.
Foilsithe / Cruthaithe: (1991)

Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.
de réir: Canet, D, et al.
Foilsithe / Cruthaithe: (2002)

Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme.
de réir: Matagne, A, et al.
Foilsithe / Cruthaithe: (2000)

Cavity hydration as a gateway to unfolding: an NMR study of hen lysozyme at high pressure and low temperature.
de réir: Kamatari, Y, et al.
Foilsithe / Cruthaithe: (2011)

Analysis of the native structure, stability and aggregation of biotinylated human lysozyme.
de réir: Minkoo Ahn, et al.
Foilsithe / Cruthaithe: (2012-01-01)

Comparison of MD simulations and NMR experiments for hen lysozyme. Analysis of local fluctuations, cooperative motions, and global changes.
de réir: Smith, L, et al.
Foilsithe / Cruthaithe: (1995)

Salt-specific effects in lysozyme solutions
de réir: T. Janc, et al.
Foilsithe / Cruthaithe: (2016-03-01)

PRODUCTION OF N-15-LABELED HEN EGG-WHITE LYSOZYME USING ASPERGILLUS-NIGER
de réir: Roberts, I, et al.
Foilsithe / Cruthaithe: (1992)

The significance of the location of mutations for the native-state dynamics of human lysozyme
de réir: Ahn, M, et al.
Foilsithe / Cruthaithe: (2016)

Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behavior in its disease-related variants.
de réir: Canet, D, et al.
Foilsithe / Cruthaithe: (1999)

Structural conformation of lysozyme layers at the air/water interface studied by neutron reflection
de réir: Lu, JR, et al.
Foilsithe / Cruthaithe: (1998)

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis.
de réir: Booth, DR, et al.
Foilsithe / Cruthaithe: (1997)

Influence of solvents on gramicidin a conformational interconversion
de réir: Bouchard, M, et al.
Foilsithe / Cruthaithe: (1998)

Asparagine and glutamine side-chain conformation in solution and crystal: a comparison for hen egg-white lysozyme using residual dipolar couplings.
de réir: Higman, V, et al.
Foilsithe / Cruthaithe: (2004)

Response of native and denatured hen lysozyme to high pressure studied by (15)N/(1)H NMR spectroscopy.
de réir: Kamatari, Y, et al.
Foilsithe / Cruthaithe: (2001)

Native-like secondary structure in a peptide from the alpha-domain of hen lysozyme.
de réir: Yang, J, et al.
Foilsithe / Cruthaithe: (1996)

Impact of the native-state stability of human lysozyme variants on protein secretion by Pichia pastoris.
de réir: Kumita, JR, et al.
Foilsithe / Cruthaithe: (2006)

Hierarchical Conformational Analysis of Native Lysozyme Based on Sub-Millisecond Molecular Dynamics Simulations.
de réir: Kai Wang, et al.
Foilsithe / Cruthaithe: (2015-01-01)

Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.
de réir: Dumoulin, M, et al.
Foilsithe / Cruthaithe: (2005)

The extracellular chaperone clusterin potently inhibits human lysozyme amyloid formation by interacting with prefibrillar species.
de réir: Kumita, JR, et al.
Foilsithe / Cruthaithe: (2007)

Effects of Protein Unfolding on Aggregation and Gelation in Lysozyme Solutions
de réir: Shakiba Nikfarjam, et al.
Foilsithe / Cruthaithe: (2020-09-01)

Lysozyme Inhibitors as Tools for Lysozyme Profiling: Identification and Antibacterial Function of Lysozymes in the Hemolymph of the Blue Mussel
de réir: Lise Vanderkelen, et al.
Foilsithe / Cruthaithe: (2023-10-01)