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- Currently displaying 26581 - 26600 of 29493 publications
Observation of surface acoustic phonon resonances: applications to the CO+O2 oscillatory reaction on Pt{100}
– Chemical Physics Letters
(1992)
191,
379
(doi: 10.1016/0009-2614(92)85395-q)
Cyclocholates: Synthesis and Ion Binding
– Tetrahedron Letters
(1992)
33,
2071
(doi: 10.1016/0040-4039(92)88145-U)
DOMINANCE OF SHORT-RANGE ORDER EFFECTS IN LEED INTENSITY SPECTRA
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203,
119
SYNTHESIS OF NOVEL ZINTL PHASES IN SUPERCRITICAL AMINES
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203,
711
RADICAL-RADICAL REACTIONS AT LOW AND VERY LOW-TEMPERATURES AND THEIR RELEVANCE TO ATMOSPHERIC CHEMISTRY
– ABSTR PAP AM CHEM S
(1992)
203,
98
The folding of an enzyme. V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies.
– J Mol Biol
(1992)
224,
837
(doi: 10.1016/0022-2836(92)90565-2)
Dissection of an enzyme by protein engineering. The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activity.
– J Mol Biol
(1992)
224,
741
(doi: 10.1016/0022-2836(92)90558-2)
The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure.
– J Mol Biol
(1992)
224,
819
(doi: 10.1016/0022-2836(92)90564-z)
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate.
– J Mol Biol
(1992)
224,
749
(doi: 10.1016/0022-2836(92)90559-3)
Histidine-aromatic interactions in barnase Elevation of histidine pKa and contribution to protein stability
– Journal of Molecular Biology
(1992)
224,
759
(doi: 10.1016/0022-2836(92)90560-7)
Isomerization of Xylenes on Boroaluminosilicate Catalysts with the ZSM-5 Structure, Synthesized in Non-alkaline Media
– Zeitschrift für Physikalische Chemie
(1992)
177,
93
The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding.
– J Mol Biol
(1992)
224,
771
(doi: 10.1016/0022-2836(92)90561-w)
The folding of an enzyme II. Substructure of barnase and the contribution of different interactions to protein stability
– Journal of Molecular Biology
(1992)
224,
783
(doi: 10.1016/0022-2836(92)90562-X)
Co-operative interactions during protein folding.
– J Mol Biol
(1992)
224,
733
(doi: 10.1016/0022-2836(92)90557-z)
The folding of an enzyme VI. The folding pathway of barnase: Comparison with theoretical models
– Journal of Molecular Biology
(1992)
224,
847
(doi: 10.1016/0022-2836(92)90566-3)
Aluminosilicate-lnduced free radical generation by murine brain glial cells in vitro: Potential significance in the aetiopathogenesis of alzheimer’s dementia
– Dementia and Geriatric Cognitive Disorders
(1992)
3,
1
(doi: 10.1159/000106985)
Core-level shift spectroscopy for adsorbates: ionic, covalent or metallic bonding?
– Chemical Physics Letters
(1992)
191,
315
(doi: 10.1016/0009-2614(92)85307-V)
Effect of alanine versus glycine in alpha-helices on protein stability.
– Nature
(1992)
356,
453
(doi: 10.1038/356453a0)
Phase behavior of disklike hard-core mesogens
– Phys Rev A
(1992)
45,
5632
(doi: 10.1103/PhysRevA.45.5632)