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- Currently displaying 26441 - 26460 of 29344 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
– 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)
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)
SYNTHESIS OF NOVEL ZINTL PHASES IN SUPERCRITICAL AMINES
– ABSTR PAP AM CHEM S
(1992)
203,
711
DOMINANCE OF SHORT-RANGE ORDER EFFECTS IN LEED INTENSITY SPECTRA
– ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203,
119
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
THE FOLDING OF AN ENZYME .4. STRUCTURE OF AN INTERMEDIATE IN THE REFOLDING OF BARNASE ANALYZED BY A PROTEIN ENGINEERING PROCEDURE
– Journal of Molecular Biology
(1992)
224,
819
(doi: 10.1016/0022-2836(92)90564-z)
ISOMERIZATION OF XYLENES ON BOROALUMINOSILICATE CATALYSTS WITH THE ZSM-5 STRUCTURE, SYNTHESIZED IN NONALKALINE MEDIA
– Zeitschrift für Physikalische Chemie
(1992)
177,
93
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)
Dissection of an enzyme by protein engineering
– J Mol Biol
(1992)
224,
741
(doi: 10.1016/0022-2836(92)90558-2)
The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed 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.
– 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)
Co-operative interactions during protein folding.
– Journal of molecular biology
(1992)
224,
733
(doi: 10.1016/0022-2836(92)90557-Z)
The folding of an enzyme II. 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)