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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)
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)
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 (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)
SYNTHESIS OF NOVEL ZINTL PHASES IN SUPERCRITICAL AMINES
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203,
711
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
– J Mol Biol
(1992)
224,
837
(doi: 10.1016/0022-2836(92)90565-2)
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
DOMINANCE OF SHORT-RANGE ORDER EFFECTS IN LEED INTENSITY SPECTRA
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203,
119
Dissection of an enzyme by protein engineering. The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activity.
– Journal of Molecular Biology
(1992)
224,
741
(doi: 10.1016/0022-2836(92)90558-2)
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 .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)
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)
The folding of an enzyme
– Journal of molecular biology
(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)
The folding of an enzyme
– Journal of molecular biology
(1992)
224,
771
(doi: 10.1016/0022-2836(92)90561-w)
Co-operative interactions during protein folding
– J Mol Biol
(1992)
224,
733
(doi: 10.1016/0022-2836(92)90557-Z)