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- Currently displaying 27241 - 27260 of 30196 publications
The detection of weak heteronuclear coupling between spin 1 and spin nuclei in MAS NMR; 14N/13C/1H triple resonance experiments
Chemical Physics Letters
(1992)
192
{379-385}
(doi: 10.1016/0009-2614(92)85486-T)
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) - PREPARATION OF THE INHERENT SPIROKETAL UNIT VIA A REVERSE COUPLING PROCESS
Synlett
(1992)
1992
399
(doi: 10.1055/s-1992-21358)
Total Synthesis of the Carboxylic Acid Ionophore Antibiotic CP-61,405 (Routiennocin)
Synlett
(1992)
1992
395
(doi: 10.1055/s-1992-21357)
HUMAN INTERLEUKIN-4 - THE SOLUTION STRUCTURE OF A 4-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 (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)
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)
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)
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. 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. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure.
J Mol Biol
(1992)
224
805
(doi: 10.1016/0022-2836(92)90563-y)
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. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure.
Journal of molecular biology
(1992)
224
819
(doi: 10.1016/0022-2836(92)90564-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. 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)
The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models.
J Mol Biol
(1992)
224
847
(doi: 10.1016/0022-2836(92)90566-3)
Co-operative interactions during protein folding.
Journal of molecular biology
(1992)
224
733
(doi: 10.1016/0022-2836(92)90557-z)
DOMINANCE OF SHORT-RANGE ORDER EFFECTS IN LEED INTENSITY SPECTRA
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203
119
