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- Currently displaying 2001 - 2020 of 2336 publications
Formation of Mixed Fibrils Demonstrates the Generic Nature and Potential Utility of Amyloid Nanostructures
Journal of the American Chemical Society
(2000)
122
12707
(doi: 10.1021/ja0029580)
%Variable-Temperature Studies of Order/Disorder Transitions in the Thiourea Pyridinium Halide Crystals by XRD and Solid-State 2H NMR
Chemistry of Materials
(2000)
12
3561
(doi: 10.1021/cm0001612)
Observation of the noncovalent assembly and disassembly pathways of the chaperone complex MtGimC by mass spectrometry.
Proceedings of the National Academy of Sciences
(2000)
97
14151
(doi: 10.1073/pnas.240326597)
Comparison of two optimization methods to derive energy parameters for protein folding: Perceptron and Z score
Proteins: Structure, Function, and Genetics
(2000)
41
192
Atmospheric aerosols as prebiotic chemical reactors.
Proceedings of the National Academy of Sciences of the United States of America
(2000)
97
11864
(doi: 10.1073/pnas.200366897)
Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell.
EMBO Journal
(2000)
19
3870
(doi: 10.1093/emboj/19.15.3870)
Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the β-domain
J Mol Biol
(2000)
300
541
(doi: 10.1006/jmbi.2000.3862)
Stabilisation of α-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding11Edited by C. R. Matthews
Journal of Molecular Biology
(2000)
300
633
(doi: 10.1006/jmbi.2000.3870)
Understanding protein folding via free-energy surfaces from theory and experiment
Trends in biochemical sciences
(2000)
25
331
A compact monomeric intermediate identified by NMR in the denaturation of dimeric triose phosphate isomerase11Edited by C. R. Matthes
J Mol Biol
(2000)
300
11
(doi: 10.1006/jmbi.2000.3834)
Toward an energy function for the contact map representation of proteins.
Proteins Structure Function and Genetics
(2000)
40
237
Detection and selective dissociation of intact ribosomes in a mass spectrometer
Proceedings of the National Academy of Sciences
(2000)
97
5185
(doi: 10.1073/pnas.97.10.5185)
Improved photo-CIDNP methods for studying protein structure and folding
J Biomol NMR
(2000)
16
235
(doi: 10.1023/a:1008351128089)
Structurally constrained protein evolution: Results from a lattice simulation
The European Physical Journal B
(2000)
15
385
(doi: 10.1007/s100510051140)
Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of transthyretin11Edited by F. E. Cohen
J Mol Biol
(2000)
297
1203
(doi: 10.1006/jmbi.2000.3600)
A statistical mechanical method to optimize energy functions for protein folding
Proceedings of the National Academy of Sciences
(2000)
97
3977
(doi: 10.1073/pnas.97.8.3977)
Mutational analysis of the propensity for amyloid formation by a globular protein
The EMBO journal
(2000)
19
1441
(doi: 10.1093/emboj/19.7.1441)
Protein folding, misfolding, and disease.
ABSTR PAP AM CHEM S
(2000)
219
U277
A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein
Biochemistry
(2000)
39
4182
(doi: 10.1021/bi991923d)
Thermal unfolding of an intermediate is associated with non-arrhenius kinetics in the folding of hen lysozyme11Edited by C. R. Matthews
Journal of molecular biology
(2000)
297
193
(doi: 10.1006/jmbi.2000.3540)