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- Currently displaying 1841 - 1860 of 2450 publications
CARB 97-One-pot direct protein glycosylation
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2006)
232
Functionalised fibrils for bio-nanotechnology
2006 INTERNATIONAL CONFERENCE ON NANOSCIENCE AND NANOTECHNOLOGY, VOLS 1 AND 2
(2006)
265
Structural interpretation of hydrogen exchange protection factors in proteins: characterization of the native state fluctuations of CI2
Structure (London, England : 1993)
(2006)
14
97
(doi: 10.1016/j.str.2005.09.012)
Determination of an ensemble of structures representing the intermediate state of the bacterial immunity protein Im7.
Proceedings of the National Academy of Sciences of the United States of America
(2005)
103
99
(doi: 10.1073/pnas.0508667102)
Structure of the Regulatory Apparatus of a Calcium-dependent Protein Kinase (CDPK): A Novel Mode of Calmodulin-target Recognition
J Mol Biol
(2005)
357
400
(doi: 10.1016/j.jmb.2005.11.093)
The importance of sequence diversity in the aggregation and evolution of proteins.
Nature
(2005)
438
878
(doi: 10.1038/nature04195)
Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alpha(s-) and beta-casein
Biochemistry
(2005)
44
17027
(doi: 10.1021/bi051352r)
Probing the pressure–temperature stability of amyloid fibrils provides new insights into their molecular properties
Biochimica et Biophysica Acta
(2005)
1764
452
(doi: 10.1016/j.bbapap.2005.10.021)
Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme.
J Mol Biol
(2005)
352
823
(doi: 10.1016/j.jmb.2005.07.040)
Transition state contact orders correlate with protein folding rates.
Journal of Molecular Biology
(2005)
352
495
(doi: 10.1016/j.jmb.2005.06.081)
Amyloid Fibril Formation Can Proceed from Different Conformations of a Partially Unfolded Protein
Biophys J
(2005)
89
4201
(doi: 10.1529/biophysj.105.068726)
Effective interactions between chaotropic agents and proteins
Proteins: Structure, Function, and Bioinformatics
(2005)
61
492
(doi: 10.1002/prot.20626)
Characterisation of Disulfide‐Bond Dynamics in Non‐Native States of Lysozyme and Its Disulfide Deletion Mutants by NMR
Chembiochem
(2005)
6
1619
(doi: 10.1002/cbic.200500196)
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates.
J Mol Biol
(2005)
351
910
(doi: 10.1016/j.jmb.2005.06.043)
Determination of the folding transition states of barnase by using ΦI-value-restrained simulations validated by double mutant ΦIJ-values
Proceedings of the National Academy of Sciences
(2005)
102
12389
(doi: 10.1073/pnas.0408226102)
Oxidative refolding of amyloidogenic variants of human lysozyme.
J Mol Biol
(2005)
351
662
(doi: 10.1016/j.jmb.2005.06.035)
A Toy Model for Predicting the Rate of Amyloid Formation from Unfolded Protein
Journal of molecular biology
(2005)
351
195
(doi: 10.1016/j.jmb.2005.05.013)
Interpreting Dynamically-Averaged Scalar Couplings in Proteins
Journal of biomolecular NMR
(2005)
32
273
(doi: 10.1007/s10858-005-8873-0)
Glycine Residues Appear to Be Evolutionarily Conserved for Their Ability to Inhibit Aggregation
Structure (London, England : 1993)
(2005)
13
1143
(doi: 10.1016/j.str.2005.04.022)
