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- Currently displaying 1961 - 1980 of 2336 publications
Pulsed NMR methods for the observation and assignment of exchangeable hydrogens: Application to bacitracin
FEBS Letters
(2001)
49
115
(doi: 10.1016/0014-5793(74)80645-9)
Temperature dependent molecular motion of a tyrosine residue of ferrocytochrome C.
FEBS letters
(2001)
70
96
(doi: 10.1016/0014-5793(76)80734-x)
A Partially Structured Species of β2-Microglobulin Is Significantly Populated under Physiological Conditions and Involved in Fibrillogenesis*
The Journal of biological chemistry
(2001)
276
46714
(doi: 10.1074/jbc.M107040200)
The Cytochrome c Fold Can Be Attained from a Compact Apo State by Occupancy of a Nascent Heme Binding Site*
The Journal of biological chemistry
(2001)
276
45813
(doi: 10.1074/jbc.M107572200)
Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules 1 1Edited by C. R. Matthews
Journal of Molecular Biology
(2001)
312
261
(doi: 10.1006/jmbi.2001.4927)
“The Mechanism of Amyloid Formation and its Links to Human Disease and Biological Evolution”, in Self-Assembling Peptide Systems in Biology, Medicine and Engineering
(2001)
65
Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain.
Journal of molecular biology
(2001)
311
325
(doi: 10.1006/jmbi.2001.4858)
Folding and Aggregation Are Selectively Influenced by the Conformational Preferences of the α-Helices of Muscle Acylphosphatase*
J Biol Chem
(2001)
276
37149
(doi: 10.1074/jbc.m105720200)
Preparation and characterization of purified amyloid fibrils [13]
Journal of the American Chemical Society
(2001)
123
8141
(doi: 10.1021/ja016229b)
Connectivity of neutral networks and structural conservation in protein
evolution
J. Mol. Evol.
(2001)
56
243
Generalized comparative modeling (GENECOMP): a combination of sequence comparison, threading, and lattice modeling for protein structure prediction and refinement.
Proteins
(2001)
44
133
(doi: 10.1002/prot.1080)
How to guarantee optimal stability for most representative structures in the Protein Data Bank.
Proteins: Structure, Function, and Bioinformatics
(2001)
44
79
(doi: 10.1002/prot.1075)
Amyloid fibril formation by a helical cytochrome
FEBS Lett
(2001)
495
184
Experimental landscapes for protein folding and misfolding.
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2001)
221
U392
Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy.
Journal of molecular biology
(2001)
307
885
(doi: 10.1006/jmbi.2001.4530)
Detection of two partially structured species in the folding process of the amyloidogenic protein beta 2-microglobulin
Journal of molecular biology
(2001)
307
379
(doi: 10.1006/jmbi.2000.4478)
Amyloid fibrils from muscle myoglobin - Even an ordinary globular protein can assume a rogue guise if conditions are right.
Nature
(2001)
410
165
(doi: 10.1038/35065514)
Pathogenesis, diagnosis and treatment of systemic amyloidosis - Discussion
PHILOS T ROY SOC B
(2001)
356
210
The structural basis of protein folding and its links with human disease
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
(2001)
356
133
(doi: 10.1098/rstb.2000.0758)
Investigating protein conformation-based inheritance and disease in yeast.
Philosophical Transactions of the Royal Society B Biological Sciences
(2001)
356
169
(doi: 10.1098/rstb.2000.0762)
