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- Currently displaying 2201 - 2220 of 2393 publications
Main-chain dynamics of a partially folded protein: N-15 NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol
Journal of molecular biology
(1996)
257
669
(doi: 10.1006/jmbi.1996.0193)
Toward a Description of the Conformations of Denatured States of Proteins. Comparison of a Random Coil Model with NMR Measurements
Journal of Physical Chemistry
(1996)
100
2661
(doi: 10.1021/jp952747v)
Analysis of Main Chain Torsion Angles in Proteins: Prediction of NMR Coupling Constants for Native and Random Coil Conformations
Journal of molecular biology
(1996)
255
494
(doi: 10.1006/jmbi.1996.0041)
The concept of a random coil: Residual structure in peptides and denatured proteins
Folding and Design
(1996)
1
R95
Collapse and cooperativity in protein folding.
Curr Opin Struct Biol
(1996)
6
31
Quenched disorder, memory, and self-organization.
Physical Review E Statistical Physics Plasmas Fluids and Related Interdisciplinary Topics
(1996)
53
R13
(doi: 10.1103/PhysRevE.53.R13)
New NMR approaches for studying protein folding.
PROG BIOPHYS MOL BIO
(1996)
65
PA417
Refolding of streptokinase domain-A restores full plasminogen-activator activity and binding capability.
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY
(1996)
65
PA451
Native-like secondary structure in a peptide from the α-domain of hen lysozyme
Folding & design
(1996)
1
473
Insights into protein dynamics by NMR techniques
DYNAMICS AND THE PROBLEM OF RECOGNITION IN BIOLOGICAL MACROMOLECULES
(1996)
288
127
Investigation of protein folding by mass spectrometry
FASEB journal : official publication of the Federation of American Societies for Experimental Biology
(1996)
10
93
(doi: 10.1096/fasebj.10.1.8566553)
"Insights into Protein Dynamics using NMR Techniques", in Dynamics and the Problem of Recognition in Biological Macromolecules
(1996)
127
Hen egg white lysozyme: A temperature dependence study of the folding process
ARCHIVES OF PHYSIOLOGY AND BIOCHEMISTRY
(1996)
104
B45
Thermodynamic unfolding of isolated streptokinase domains.
PROG BIOPHYS MOL BIO
(1996)
65
PA416
Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin.
Journal of Molecular Biology
(1995)
253
651
(doi: 10.1006/jmbi.1995.0579)
Following protein folding in real time using NMR spectroscopy.
Nature Structural & Molecular Biology
(1995)
2
865
(doi: 10.1038/nsb1095-865)
Structural basis of the stability of a lysozyme molten globule
Nature Structural Biology
(1995)
2
871
(doi: 10.1038/nsb1095-871)
Conformational properties of four peptides spanning the sequence of hen lysozyme.
Journal of molecular biology
(1995)
252
483
(doi: 10.1006/jmbi.1995.0513)
The crystal structure of the catalytic domain of human urokinase-type plasminogen activator
Structure
(1995)
3
681
A Ca(2+)-binding chimera of human lysozyme and bovine alpha-lactalbumin that can form a molten globule.
J Biol Chem
(1995)
270
10514
(doi: 10.1074/jbc.270.18.10514)