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- Currently displaying 28141 - 28160 of 31086 publications
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 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)
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)
DOMINANCE OF SHORT-RANGE ORDER EFFECTS IN LEED INTENSITY SPECTRA
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203
119
The folding of an enzyme II. Substructure of barnase and the contribution of different interactions to protein stability
J Mol Biol
(1992)
224
783
(doi: 10.1016/0022-2836(92)90562-X)
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)
RADICAL-RADICAL REACTIONS AT LOW AND VERY LOW-TEMPERATURES AND THEIR RELEVANCE TO ATMOSPHERIC CHEMISTRY
ABSTR PAP AM CHEM S
(1992)
203
98
The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding.
J Mol Biol
(1992)
224
771
(doi: 10.1016/0022-2836(92)90561-w)
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)
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)
Co-operative interactions during protein folding
Journal of Molecular Biology
(1992)
224
733
(doi: 10.1016/0022-2836(92)90557-z)
SYNTHESIS OF NOVEL ZINTL PHASES IN SUPERCRITICAL AMINES
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203
711
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)
