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- Currently displaying 26401 - 26420 of 29271 publications
CUMULATIVE REACTION PROBABILITIES FOR H+H2-]H2+H FROM A KNOWLEDGE OF THE ANHARMONIC-FORCE FIELD
Chemical Physics Letters
(1992)
192
407
(doi: 10.1016/0009-2614(92)85491-R)
A digital interface for phase control of PTS-300 synthesizers
Journal of Magnetic Resonance (1969)
(1992)
97
607
(doi: 10.1016/0022-2364(92)90039-a)
Total Synthesis of the Carboxylic Acid Ionophore Antibiotic CP-61,405 (Routiennocin)
Synlett
(1992)
1992
395
(doi: 10.1055/s-1992-21357)
Total Synthesis of the Carboxylic Acid lonophore Antibiotic CP-61,405 (Routiennocin): Preparation of the Inherent Spiroketal Unit via a Reverse Coupling Process
Synlett
(1992)
1992
399
(doi: 10.1055/s-1992-21358)
Human interleukin 4. The solution structure of a four-helix bundle protein.
J Mol Biol
(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 .3. STRUCTURE OF THE TRANSITION-STATE FOR UNFOLDING OF BARNASE ANALYZED BY A PROTEIN ENGINEERING PROCEDURE
Journal of Molecular Biology
(1992)
224
805
(doi: 10.1016/0022-2836(92)90563-y)
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)
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. 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)
The folding of an enzyme I. 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
Journal of molecular biology
(1992)
224
783
(doi: 10.1016/0022-2836(92)90562-x)
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 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)
Isomerization of Xylenes on Boroaluminosilicate Catalysts with the ZSM-5 Structure, Synthesized in Non-alkaline Media
Zeitschrift für Physikalische Chemie
(1992)
177
93
