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- Currently displaying 1761 - 1780 of 2520 publications
Structure, dynamics and folding of an immunoglobulin domain of the gelation factor (ABP-120) from Dictyostelium discoideum.
J Mol Biol
(2009)
388
865
(doi: 10.1016/j.jmb.2009.02.063)
Toward an accurate determination of free energy landscapes in solution states of proteins
Journal of the American Chemical Society
(2009)
131
3810
(doi: 10.1021/ja8087295)
The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints.
Nature Structural and Molecular Biology
(2009)
16
318
(doi: 10.1038/nsmb.1562)
Structural Investigation of an SH3 Amyloid Protein Fibril
Biophysical Journal
(2009)
96
86A
(doi: 10.1016/j.bpj.2008.12.351)
Factors that affect the degree of twist in β-sheet structures: A Molecular dynamics simulation study of a cross-β filament of the GNNQQNY peptide
J Phys Chem B
(2009)
113
1728
(doi: 10.1021/jp8078259)
H-1, N-15 and C-13 assignments of yellow fluorescent protein (YFP) Venus
Biomol NMR Assign
(2009)
3
67
(doi: 10.1007/s12104-009-9143-y)
Similarities in the thermodynamics and kinetics of aggregation of disease‐related Aβ(1–40) peptides
Protein Sci
(2009)
16
1214
(doi: 10.1110/ps.062734207)
Molecular determinants of the aggregation behavior of alpha- and beta-synuclein
Protein Sci
(2009)
17
887
(doi: 10.1110/ps.073181508)
Observation of sequence specificity in the seeding of protein amyloid fibrils.
Protein Sci
(2009)
13
1933
(doi: 10.1110/ps.04707004)
Chemical modification of insulin in amyloid fibrils.
Protein science : a publication of the Protein Society
(2009)
12
2637
(doi: 10.1110/ps.0360403)
Enthalpic and entropic contributions mediate the role of disulfide bonds on the conformational stability of Interleukin-4
Protein science : a publication of the Protein Society
(2009)
15
33
(doi: 10.1110/ps.051593306)
Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspB.
Protein science : a publication of the Protein Society
(2008)
8
1350
(doi: 10.1110/ps.8.6.1350)
Expression and characterization of the intact N-terminal domain of streptokinase.
Protein Sci
(2008)
8
443
(doi: 10.1110/ps.8.2.443)
Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.
Protein Science
(2008)
6
1316
(doi: 10.1002/pro.5560060620)
A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding.
Protein Science
(2008)
10
1216
(doi: 10.1110/ps.52801)
Analysis of the interactions between streptokinase domains and human plasminogen
Protein Sci
(2008)
7
2190
(doi: 10.1002/pro.5560071017)
Selective association of protein molecules followed by mass spectrometry
Protein Sci
(2008)
8
1368
(doi: 10.1110/ps.8.6.1368)
The domain organization of streptokinase: nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments.
Protein Science
(2008)
5
693
(doi: 10.1002/pro.5560050414)
Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonance.
Protein science : a publication of the Protein Society
(2008)
5
2583
(doi: 10.1002/pro.5560051221)