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- Currently displaying 27701 - 27720 of 30657 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)
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 (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)
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
Journal of molecular biology
(1992)
224
771
(doi: 10.1016/0022-2836(92)90561-w)
Histidine-aromatic interactions in barnase
Journal of Molecular Biology
(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)
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 .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)
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate
Journal of molecular biology
(1992)
224
749
(doi: 10.1016/0022-2836(92)90559-3)
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)
The folding of an enzyme
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.
Journal of molecular biology
(1992)
224
819
(doi: 10.1016/0022-2836(92)90564-Z)
RADICAL-RADICAL REACTIONS AT LOW AND VERY LOW-TEMPERATURES AND THEIR RELEVANCE TO ATMOSPHERIC CHEMISTRY
ABSTR PAP AM CHEM S
(1992)
203
98
SYNTHESIS OF NOVEL ZINTL PHASES IN SUPERCRITICAL AMINES
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203
711
DOMINANCE OF SHORT-RANGE ORDER EFFECTS IN LEED INTENSITY SPECTRA
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203
119
ISOMERIZATION OF XYLENES ON BOROALUMINOSILICATE CATALYSTS WITH THE ZSM-5 STRUCTURE, SYNTHESIZED IN NONALKALINE MEDIA
Zeitschrift für Physikalische Chemie
(1992)
177
93
