Tips on using this search form
- All search terms are case-insensitive
- If you specify more than one search option (e.g. you search for both "Authors" and "Paper title") then the publications returned will be those that match all of your search terms
- To reset the search form, click here
- Currently displaying 2021 - 2040 of 2393 publications
Pulsed NMR methods for the observation and assignment of exchangeable hydrogens: application to bacitracin.
FEBS Lett
(2001)
49
115
(doi: 10.1016/0014-5793(74)80645-9)
Conformation mobility within the structure of muscular parvalbumins. An NMR study of the aromatic resonances of phenylalanine residues.
FEBS Letters
(2001)
65
190
(doi: 10.1016/0014-5793(76)80477-2)
Assignment of aromatic amino acid PMR resonances of horse ferricytochrome c.
FEBS Letters
(2001)
51
60
(doi: 10.1016/0014-5793(75)80854-4)
A P-31 MAS NMR-STUDY OF CYTIDINE 2'-PHOSPHATE BOUND TO RIBONUCLEASE-A IN THE CRYSTALLINE STATE
FEBS Lett
(2001)
225
183
(doi: 10.1016/0014-5793(87)81154-7)
A partially structured species of β2-microglobulin is significantly populated under physiological conditions and involved in fibrillogenesis
J Biol Chem
(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.
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.
J Mol Biol
(2001)
311
325
(doi: 10.1006/jmbi.2001.4858)
Protein folding and its links with human disease.
Biochem Soc Symp
(2001)
68
1
(doi: 10.1042/bss0680001)
Folding and Aggregation are Selectively Influenced by the Conformational Preferences of the α-Helices of Muscle Acylphosphatase
The Journal of biological chemistry
(2001)
276
37149
(doi: 10.1074/jbc.M105720200)
Preparation and characterization of purified amyloid fibrils.
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 Structure Function and Genetics
(2001)
44
133
(doi: 10.1002/prot.1080)
How to guarantee optimal stability for most representative structures in the protein data bank
Proteins
(2001)
44
79
(doi: 10.1002/prot.1075)
Amyloid fibril formation by a helical cytochrome
FEBS letters
(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 β2-microglobulin11Edited by C. R. Matthews
Journal of Molecular Biology
(2001)
307
379
(doi: 10.1006/jmbi.2000.4478)
