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- Currently displaying 28201 - 28220 of 31149 publications
HUMAN INTERLEUKIN-4 - THE SOLUTION STRUCTURE OF A 4-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)
Preliminary communication: Unexpected length dependence of die solubility of chain molecules
Molecular Physics
(1992)
75
983
(doi: 10.1080/00268979200100761)
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)
Cyclocholates: Synthesis and Ion Binding
Tetrahedron Letters
(1992)
33
2071
(doi: 10.1016/0040-4039(92)88145-U)
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)
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)
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
Co-operative interactions during protein folding.
J Mol Biol
(1992)
224
733
(doi: 10.1016/0022-2836(92)90557-Z)
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 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)
The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure.
J Mol Biol
(1992)
224
819
(doi: 10.1016/0022-2836(92)90564-Z)
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)
DOMINANCE OF SHORT-RANGE ORDER EFFECTS IN LEED INTENSITY SPECTRA
ABSTR PAP AM CHEM S
(1992)
203
119
SYNTHESIS OF NOVEL ZINTL PHASES IN SUPERCRITICAL AMINES
ABSTR PAP AM CHEM S
(1992)
203
711
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 .1. 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)
Isomerization of Xylenes on Boroaluminosilicate Catalysts with the ZSM-5 Structure, Synthesized in Non-alkaline Media
Zeitschrift für Physikalische Chemie
(1992)
177
93
Core-level shift spectroscopy for adsorbates: ionic, covalent or metallic bonding?
Chemical Physics Letters
(1992)
191
315
(doi: 10.1016/0009-2614(92)85307-V)
