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- Currently displaying 27441 - 27460 of 30391 publications
Human interleukin 4. The solution structure of a four-helix bundle protein
Journal of molecular biology
(1992)
224
899
(doi: 10.1016/0022-2836(92)90457-u)
INFRARED ULTRAVIOLET DOUBLE-RESONANCE MEASUREMENTS ON THE RELAXATION OF ROTATIONAL ENERGY IN THE (3(1), 2(1)4(1)5(1)) FERMI RESONANCE STATES OF C2H2
Chemical Physics Letters
(1992)
191
574
(doi: 10.1016/0009-2614(92)85591-W)
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)
Unexpected length dependence of the solubility of chain molecules
Molecular Physics
(1992)
75
983
(doi: 10.1080/00268979200100761)
Cyclocholates: Synthesis and Ion Binding
Tetrahedron Letters
(1992)
33
2071
(doi: 10.1016/0040-4039(92)88145-U)
THE FOLDING OF AN ENZYME .5. H/H-2 EXCHANGE NUCLEAR-MAGNETIC-RESONANCE STUDIES ON THE FOLDING PATHWAY OF BARNASE - COMPLEMENTARITY TO AND AGREEMENT WITH PROTEIN ENGINEERING STUDIES
Journal of molecular biology
(1992)
224
837
(doi: 10.1016/0022-2836(92)90565-2)
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate.
Journal of molecular biology
(1992)
224
749
(doi: 10.1016/0022-2836(92)90559-3)
THE FOLDING OF AN ENZYME .1. THEORY OF PROTEIN ENGINEERING ANALYSIS OF STABILITY AND PATHWAY OF PROTEIN FOLDING
Journal of molecular biology
(1992)
224
771
(doi: 10.1016/0022-2836(92)90561-W)
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)
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)
Co-operative interactions during protein folding.
Journal of molecular biology
(1992)
224
733
(doi: 10.1016/0022-2836(92)90557-z)
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 .2. 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)
The folding of an enzyme
Journal of molecular biology
(1992)
224
819
(doi: 10.1016/0022-2836(92)90564-Z)
Isomerization of Xylenes on Boroaluminosilicate Catalysts with the ZSM-5 Structure, Synthesized in Non-alkaline Media
Zeitschrift für Physikalische Chemie
(1992)
177
93
DOMINANCE OF SHORT-RANGE ORDER EFFECTS IN LEED INTENSITY SPECTRA
ABSTR PAP AM CHEM S
(1992)
203
119
RADICAL-RADICAL REACTIONS AT LOW AND VERY LOW-TEMPERATURES AND THEIR RELEVANCE TO ATMOSPHERIC CHEMISTRY
ABSTR PAP AM CHEM S
(1992)
203
98
SYNTHESIS OF NOVEL ZINTL PHASES IN SUPERCRITICAL AMINES
ABSTR PAP AM CHEM S
(1992)
203
711
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)
