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- Currently displaying 27681 - 27700 of 30637 publications
A NEAR-EDGE X-RAY ABSORPTION FINE-STRUCTURE AND PHOTOELECTRON SPECTROSCOPIC STUDY OF THE STRUCTURE OF ACETYLENE ON PD(111) AT LOW-TEMPERATURE
Surface Science
(1992)
268
1
(doi: 10.1016/0039-6028(92)90945-3)
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 (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
Journal of Molecular Biology
(1992)
224
749
(doi: 10.1016/0022-2836(92)90559-3)
Co-operative interactions during protein folding.
J Mol Biol
(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.
Journal of Molecular Biology
(1992)
224
741
(doi: 10.1016/0022-2836(92)90558-2)
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 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. 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)
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)
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)
The folding of an enzyme V. solH2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: Complementarity to and agreement with protein engineering studies
Journal of Molecular Biology
(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.
Journal of molecular biology
(1992)
224
847
(doi: 10.1016/0022-2836(92)90566-3)
ISOMERIZATION OF XYLENES ON BOROALUMINOSILICATE CATALYSTS WITH THE ZSM-5 STRUCTURE, SYNTHESIZED IN NONALKALINE MEDIA
Zeitschrift für Physikalische Chemie
(1992)
177
93
RADICAL-RADICAL REACTIONS AT LOW AND VERY LOW-TEMPERATURES AND THEIR RELEVANCE TO ATMOSPHERIC CHEMISTRY
ABSTR PAP AM CHEM S
(1992)
203
98
DOMINANCE OF SHORT-RANGE ORDER EFFECTS IN LEED INTENSITY SPECTRA
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(1992)
203
119
