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- Currently displaying 2141 - 2160 of 2350 publications
Nuclear magnetic resonance studies of blood platelets.
Philosophical transactions of the Royal Society of London. Series B, Biological sciences
(1997)
289
413
(doi: 10.1098/rstb.1980.0058)
The effects of guanidine hydrochloride on the 'random coil' conformations and NMR chemical shifts of the peptide series GGXGG
Journal of biomolecular NMR
(1997)
10
221
(doi: 10.1023/A:1018340217891)
Proton magnetic resonance studies of the tyrosine residues of hen lysozyme-assignment and detection of conformational mobility
Proceedings of the Royal Society of London Biological Sciences
(1997)
189
503
(doi: 10.1098/rspb.1975.0070)
Nuclear magnetic resonance studies on the structure of lysozyme in solution
Proceedings of the Royal Society of London. A. Mathematical and Physical Sciences
(1997)
345
41
(doi: 10.1098/rspa.1975.0124)
Preface
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
(1997)
348
3
(doi: 10.1098/rstb.1995.0038)
Insights into protein folding using physical techniques: studies of lysozyme and α-lactalbumin
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
(1997)
348
17
(doi: 10.1098/rstb.1995.0041)
Recovery of protein structure from contact maps.
Folding & design
(1997)
2
295
ASSIGNMENT OF H-1 NMR-SPECTRA OF PROTEINS
Proceedings of the Royal Society of London. A. Mathematical and Physical Sciences
(1997)
345
23
(doi: 10.1098/rspa.1975.0123)
Studies of exchangeable hydrogens in lysozyme by means of Fourier transform proton magnetic resonance.
Proceedings of the Royal Society of London. Series B. Biological Sciences
(1997)
189
485
(doi: 10.1098/rspb.1975.0069)
Characterisation of protein unfolding by NMR diffusion measurements
Journal of Biomolecular NMR
(1997)
10
199
(doi: 10.1023/a:1018304117895)
Model of correlated evolution.
Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics
(1996)
54
6053
(doi: 10.1103/PhysRevE.54.6053)
Protein folding monitored at individual residues during a two-dimensional NMR experiment
Science (New York, N.Y.)
(1996)
274
1161
Time-resolved biophysical methods in the study of protein folding.
Curr Opin Struct Biol
(1996)
6
630
Rapid refolding of a proline-rich all-beta-sheet fibronectin type III module.
Proc Natl Acad Sci U S A
(1996)
93
10703
(doi: 10.1073/pnas.93.20.10703)
Probing the Nature of Noncovalent Interactions by Mass Spectrometry. A Study of Protein−CoA Ligand Binding and Assembly
Journal of the American Chemical Society
(1996)
118
8646
(doi: 10.1021/ja960211x)
Molecular characterisation of a thermoactive beta-1,3-glucanase from Oerskovia xanthineolytica
Biochimica et biophysica acta
(1996)
1296
145
(doi: 10.1016/0167-4838(96)00062-3)
Insight into a random coil conformation and an isolated helix: structural and dynamical characterisation of the C-helix peptide from hen lysozyme.
J Mol Biol
(1996)
261
443
(doi: 10.1006/jmbi.1996.0475)
Isotope-Labeling Strategy for the Assignment of Protein Fragments Generated for Mass Spectrometry
Journal of the American Chemical Society
(1996)
118
7402
(doi: 10.1021/ja9531236)