Entry ID |
Link Type |
Entity ID |
Title |
568
|
Sequence mapping |
1 |
Applications of Natural-Abundance Carbon-13 NMR to Studies of Proteins and
Glycoproteins |
569
|
Sequence mapping |
1 |
A Structural Study of the Hydrophobic Box Region of Lysozyme in Solution Using
Nuclear Overhauser Effects |
791
|
Sequence mapping |
1 |
Proton NMR Detection of Long-Range Heteronuclear Multiquantum Coherences in
Proteins: The Complete Assignment of the Quaternary Aromatic 13C Shifts in
Lysozyme |
1093
|
Sequence mapping |
1 |
Sequential 1H NMR Assignments and Secondary Structure of Hen Egg White Lysozyme
in Solution |
1104
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance
Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
1105
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance
Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
1650
|
Sequence mapping |
1 |
Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of
Chemical Shifts in NMR Spectra of Denatured States of Lysozyme |
1651
|
Sequence mapping |
1 |
Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of
Chemical Shifts in NMR Spectra of Denatured States of Lysozyme |
1653
|
Sequence mapping |
1 |
Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of
Chemical Shifts in NMR Spectra of Denatured States of Lysozyme |
1770
|
Sequence mapping |
1 |
1H-NMR Study of the Intramolecular Interaction of a Substrate Analogue
Covalently Attached to Aspartic Acid-101 in Lysozyme |
1772
|
Sequence mapping |
1 |
1H-NMR Study of the Intramolecular Interaction of a Substrate Analogue
Covalently Attached to Aspartic Acid-101 in Lysozyme |
1798
|
Sequence mapping |
1 |
Effect of inhibitors on conformational changes in hen lysozyme around thermal
transition point in solution and solid state |
1799
|
Sequence mapping |
1 |
Effect of inhibitors on conformational changes in hen lysozyme around thermal
transition point in solution and solid state |
1800
|
Sequence mapping |
1 |
Effect of inhibitors on conformational changes in hen lysozyme around thermal
transition point in solution and solid state |
1801
|
Sequence mapping |
1 |
Effect of inhibitors on conformational changes in hen lysozyme around thermal
transition point in solution and solid state |
1802
|
Sequence mapping |
1 |
Effect of inhibitors on conformational changes in hen lysozyme around thermal
transition point in solution and solid state |
1803
|
Sequence mapping |
1 |
Effect of inhibitors on conformational changes in hen lysozyme around thermal
transition point in solution and solid state |
1865
|
Sequence mapping |
1 |
Studies of Individual Carbon Sites of Hen Egg White Lysozyme by Natural
Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy |
1881
|
Sequence mapping |
1 |
Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of
Chemical Shifts in NMR Spectra of Denatured States of Lysozyme |
1882
|
Sequence mapping |
1 |
Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of
Chemical Shifts in NMR Spectra of Denatured States of Lysozyme |
1883
|
Sequence mapping |
1 |
Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of
Chemical Shifts in NMR Spectra of Denatured States of Lysozyme |
1884
|
Sequence mapping |
1 |
Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of
Chemical Shifts in NMR Spectra of Denatured States of Lysozyme |
1975
|
Sequence mapping |
1 |
N.m.r. study of conformational changes in lysozyme around the thermal transition
point |
1977
|
Sequence mapping |
1 |
N.m.r. study of conformational changes in lysozyme around the thermal transition
point |
2231
|
Sequence mapping |
1 |
Preparation of a Lysozyme Derivative in Which Two Domains Are Cross-Linked
Intramolecularly between Trp62 and Asp101 |
2446
|
Sequence mapping |
1 |
Studies of beta-Sheet Structure in Lysozyme by Proton Nuclear Magnetic
Resonance. Assignments and Analysis of Spin-Spin Coupling Constants |
2786
|
Sequence mapping |
1 |
Complete Assignment of Aromatic 1H Nuclear Magnetic Resonances of the Tyrosine
Residues of Hen Lysozyme |
2858
|
Sequence mapping |
1 |
Comparisons of Ring-Current Shifts Calculated from the Crystal Structure of Egg
White Lysozyme of Hen with the Proton Nuclear Magnetic Resonance Spectrum of
Lysozyme in Solution |
2917
|
Sequence mapping |
1 |
Study of Tryptophan Residues of Lysozyme Using 1H Nuclear Magnetic Resonance |
2957
|
Sequence mapping |
1 |
Complete Assignment of the 1H NMR Spectrum of the Aromatic Residues of Lysozyme |
4562
|
Sequence mapping |
1 |
1H and 13C chemical shift assignments of native hen egg white lysozyme |
4943
|
Sequence mapping |
1 |
1H Chemical shift Assignments for Lysozymes marketed by Seikagaku and Sigma
companies at pH 3.8, 308K |
5068
|
Sequence mapping |
1 |
Recombinant hen lysozyme containing the extra N-terminal Met as the standard
reference for the study of hen lysozyme variants |
5069
|
Sequence mapping |
1 |
NMR Structural Study of Two-Disulfide Variant of hen Lysozyme: 2SS[6-127,
30-115]-A Disulfide Intermediate with a Partly Unfolded Structure |
7144
|
Sequence mapping |
1 |
Chemical shift changes upon ligand binding |
7159
|
Sequence mapping |
1 |
1H chemical shift assignments of 2SS[6-127, 30-115] at pH 3.8 and 25 C |
7160
|
Sequence mapping |
1 |
1H chemical shift assignments of metLYZ at pH 3.8 and 25 C |
18304
|
Sequence mapping |
1 |
Order parameters for HEWL |
18305
|
Sequence mapping |
1 |
Order parameters for HEWL-chitotriose |