Structure of hen lysozyme in solution.

Structure of hen lysozyme in solution.

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...

Bibliográfalaš dieđut
Váldodahkkit:	Smith, L, Sutcliffe, M, Redfield, C, Dobson, C
Materiálatiipa:	Journal article
Giella:	English
Almmustuhtton:	1993

Geahča maid

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

A refined solution structure of hen lysozyme determined using residual dipolar coupling data.
Dahkki: Schwalbe, H, et al.
Almmustuhtton: (2001)

Native-like secondary structure in a peptide from the alpha-domain of hen lysozyme.
Dahkki: Yang, J, et al.
Almmustuhtton: (1996)

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

The conformation of lysozyme in solution
Dahkki: Dobson, C, et al.
Almmustuhtton: (1975)

The origin of the alpha-domain intermediate in the folding of hen lysozyme.
Dahkki: Matagne, A, et al.
Almmustuhtton: (1998)

Characterisation of the dominant oxidative folding intermediate of hen lysozyme.
Dahkki: van den Berg, B, et al.
Almmustuhtton: (1999)

Conformational fluctuations of hen lysozyme investigated by high pressure NMR spectroscopy
Dahkki: Kamatari, Y, et al.
Almmustuhtton: (2003)

Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme.
Dahkki: Eyles, S, et al.
Almmustuhtton: (1994)

Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy.
Dahkki: Chamberlain, A, et al.
Almmustuhtton: (2001)

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

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

The oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase.
Dahkki: van den Berg, B, et al.
Almmustuhtton: (1999)

Molecular dynamics simulations of peptide fragments from hen lysozyme: insight into non-native protein conformations.
Dahkki: Smith, L, et al.
Almmustuhtton: (1998)

Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme.
Dahkki: Matagne, A, et al.
Almmustuhtton: (2000)

Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.
Dahkki: Johnson, R, et al.
Almmustuhtton: (2005)

Comparison of MD simulations and NMR experiments for hen lysozyme. Analysis of local fluctuations, cooperative motions, and global changes.
Dahkki: Smith, L, et al.
Almmustuhtton: (1995)

The dynamics of lysozyme from bacteriophage lambda in solution probed by NMR and MD simulations.
Dahkki: Smith, L, et al.
Almmustuhtton: (2013)

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

The solution dynamics of amyloidogenic Asp67His variant of human lysozyme: Insights from hydrogen exchange
Dahkki: Canet, D, et al.
Almmustuhtton: (2000)

PRODUCTION OF N-15-LABELED HEN EGG-WHITE LYSOZYME USING ASPERGILLUS-NIGER
Dahkki: Roberts, I, et al.
Almmustuhtton: (1992)

NMR studies of the dynamics and the folding of hen lysozyme
Dahkki: Buck, M, et al.
Almmustuhtton: (1994)

ISOLATION AND PURIFICATION OF LYSOZYME FROM THE HEN EGG WHITE
Dahkki: S. S., et al.
Almmustuhtton: (2015-12-01)

Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.
Dahkki: Canet, D, et al.
Almmustuhtton: (2002)

Oxidative refolding of amyloidogenic variants of human lysozyme.
Dahkki: Wain, R, et al.
Almmustuhtton: (2005)

Interaction between Sorbitol and Hen Egg White Lysozyme: From Dynamics to Structure
Dahkki: Mohammad Reza Ramezani, et al.
Almmustuhtton: (2016-11-01)

Prolonged glycation of hen egg white lysozyme generates non amyloidal structures.
Dahkki: Sudeshna Ghosh, et al.
Almmustuhtton: (2013-01-01)

A near-native state on the slow refolding pathway of hen lysozyme.
Dahkki: Kulkarni, S, et al.
Almmustuhtton: (1999)

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

Lysozyme sources for disease prevention and health promotion – Donkey milk in alternative to hen egg-white lysozyme
Dahkki: Vita Maria Marino, et al.
Almmustuhtton: (2024-06-01)

Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain.
Dahkki: Krebs, MR, et al.
Almmustuhtton: (2000)

Expression of recombinant human lysozyme in egg whites of transgenic hens.
Dahkki: Dainan Cao, et al.
Almmustuhtton: (2015-01-01)

Safety evaluation of the food enzyme lysozyme from hens' eggs
Dahkki: EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), et al.
Almmustuhtton: (2023-04-01)

Safety evaluation of the food enzyme lysozyme from hens' eggs
Dahkki: EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP), et al.
Almmustuhtton: (2023-03-01)

Molecular dynamics simulation or structure refinement of proteins: are solvent molecules required? a case study using hen lysozyme
Dahkki: Pechlaner, M, et al.
Almmustuhtton: (2022)

Structure of hen egg-white lysozyme solvated in TFE/water: a molecular dynamics simulation study based on NMR data.
Dahkki: Eichenberger, A, et al.
Almmustuhtton: (2013)

Structure of hen egg-white lysozyme solvated in TFE/water: a molecular dynamics simulation study based on NMR data
Dahkki: Eichenberger, A, et al.
Almmustuhtton: (2013)

Independent nucleation and heterogeneous assembly of structure during folding of equine lysozyme.
Dahkki: Morozova-Roche, L, et al.
Almmustuhtton: (1999)

Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.
Dahkki: Dumoulin, M, et al.
Almmustuhtton: (2005)

Research advancements in the purification technology and application of hen egg white lysozyme
Dahkki: Liang-Liang Chen, et al.
Almmustuhtton: (2024-12-01)