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- Currently displaying 2701 - 2720 of 2922 publications
Structural and Dynamical Properties of a Denatured Protein. Heteronuclear 3D NMR Experiments and Theoretical Simulations of Lysozyme in 8 M Urea †
– Biochemistry
(1997)
36,
8977
(DOI: 10.1021/bi970049q)
Detection of residue contacts in a protein folding intermediate.
– Proceedings of the National Academy of Sciences
(1997)
94,
7182
(DOI: 10.1073/pnas.94.14.7182)
Stopped-Flow Photo-CIDNP Observation of Protein Folding
– Journal of the American Chemical Society
(1997)
119,
5049
(DOI: 10.1021/ja9644135)
Structural characterisation and comparison of the native and A-states of equine lysozyme.
– J Mol Biol
(1997)
268,
903
(DOI: 10.1006/jmbi.1997.0996)
Stability threshold as a selection principle for protein design
– Physical Review Letters
(1997)
78,
3967
(DOI: 10.1103/physrevlett.78.3967)
Fast and slow tracks in lysozyme folding: insight into the role of domains in the folding process11Edited by P. E. Wright
– Journal of Molecular Biology
(1997)
267,
1068
(DOI: 10.1006/jmbi.1997.0963)
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
– Nature
(1997)
385,
787
(DOI: 10.1038/385787a0)
Modified configurational bias Monte Carlo method for simulation of polymer systems
– Journal of Chemical Physics
(1997)
106,
2970
(DOI: 10.1063/1.473356)
Folding and binding from theory to therapy - Editorial overview
– Current opinion in structural biology
(1997)
7,
1
“ The Role of NMR Spectroscopy in Understanding How Proteins Fold”, in Biological NMR Spectroscopy
(1997)
82
Acceleration of the folding of hen lysozyme by trifluoroethanol
– J Mol Biol
(1997)
265,
112
(DOI: 10.1006/jmbi.1996.0715)
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)
Nuclear magnetic resonance studies on the structure of lysozyme in solution
– Proceedings of the Royal Society A
(1997)
345,
41
(DOI: 10.1098/rspa.1975.0124)
Proton magnetic resonance studies of the tyrosine residues of hen lysozyme-assignment and detection of conformational mobility.
– Proc R Soc Lond B Biol Sci
(1997)
189,
503
(DOI: 10.1098/rspb.1975.0070)
ASSIGNMENT OF H-1 NMR-SPECTRA OF PROTEINS
– Proceedings of the Royal Society A
(1997)
345,
23
(DOI: 10.1098/rspa.1975.0123)
Characterisation of protein unfolding by NMR diffusion measurements
– Journal of Biomolecular NMR
(1997)
10,
199
(DOI: 10.1023/A:1018304117895)
Studies of exchangeable hydrogens in lysozyme by means of Fourier transform proton magnetic resonance
– Proc R Soc Lond B Biol Sci
(1997)
189,
485
(DOI: 10.1098/rspb.1975.0069)
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)
Preface
– Philosophical Transactions of the Royal Society B Biological Sciences
(1997)
348,
3
(DOI: 10.1098/rstb.1995.0038)
Recovery of protein structure from contact maps.
– Folding and Design
(1997)
2,
295