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- Currently displaying 26501 - 26520 of 29408 publications
Total Synthesis of the Carboxylic Acid Ionophore Antibiotic CP-61,405 (Routiennocin)
– Synlett
(1992)
1992,
395
(doi: 10.1055/s-1992-21357)
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)
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)
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. V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies.
– J Mol Biol
(1992)
224,
837
(doi: 10.1016/0022-2836(92)90565-2)
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
Histidine-aromatic interactions in barnase
– Journal of Molecular Biology
(1992)
224,
759
(doi: 10.1016/0022-2836(92)90560-7)
ISOMERIZATION OF XYLENES ON BOROALUMINOSILICATE CATALYSTS WITH THE ZSM-5 STRUCTURE, SYNTHESIZED IN NONALKALINE MEDIA
– Zeitschrift für Physikalische Chemie
(1992)
177,
93
Dissection of an enzyme by protein engineering
– Journal of molecular biology
(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.
– J Mol Biol
(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
– Journal of Molecular Biology
(1992)
224,
819
(doi: 10.1016/0022-2836(92)90564-z)
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 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
– Journal of molecular biology
(1992)
224,
783
(doi: 10.1016/0022-2836(92)90562-x)
Co-operative interactions during protein folding
– Journal of molecular biology
(1992)
224,
733
(doi: 10.1016/0022-2836(92)90557-Z)