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- Currently displaying 27181 - 27200 of 30130 publications
Infrared—ultraviolet double resonance measurements on the relaxation of rotational energy in the (31, 214151) 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)
Preliminary communication: Unexpected length dependence of die 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 .4. STRUCTURE OF AN INTERMEDIATE IN THE REFOLDING OF BARNASE ANALYZED BY A PROTEIN ENGINEERING PROCEDURE
J Mol Biol
(1992)
224
819
(doi: 10.1016/0022-2836(92)90564-Z)
Dissection of an enzyme by protein engineering
J Mol Biol
(1992)
224
741
(doi: 10.1016/0022-2836(92)90558-2)
Co-operative interactions during protein folding.
Journal of Molecular Biology
(1992)
224
733
(doi: 10.1016/0022-2836(92)90557-z)
THE FOLDING OF AN ENZYME .6. THE FOLDING PATHWAY OF BARNASE - COMPARISON WITH THEORETICAL-MODELS
Journal of molecular biology
(1992)
224
847
(doi: 10.1016/0022-2836(92)90566-3)
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.
J Mol Biol
(1992)
224
759
(doi: 10.1016/0022-2836(92)90560-7)
The folding of an enzyme V. solH2H 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)
The folding of an enzyme
Journal of molecular biology
(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)
THE FOLDING OF AN ENZYME .3. STRUCTURE OF THE TRANSITION-STATE FOR UNFOLDING OF BARNASE ANALYZED BY A PROTEIN ENGINEERING PROCEDURE
J Mol Biol
(1992)
224
805
(doi: 10.1016/0022-2836(92)90563-y)
ISOMERIZATION OF XYLENES ON BOROALUMINOSILICATE CATALYSTS WITH THE ZSM-5 STRUCTURE, SYNTHESIZED IN NONALKALINE 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
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
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203
98
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)
