Results 221 to 230 of about 181,206 (262)

Stabilization of the peptide conformation on the micellar surface

The Analyst, 1994
The conformational mobility of peptide molecules plays a significant role in peptide-receptor interactions and quantitative structure-activity relationships. As a receptor mimetic system, bis(2-ethylhexyl) sodium succinate (AOT) reversed micelles containing an aqueous solution of one of the melanotrophine inhibiting factor analogues prolyltyrosyl ...
, Shapiro YuE, , Gorbatyuk VYa, A A, Mazurov, S A, Andronati   +3 more
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Effect of conformability on grasp static stability

Proceedings 2001 ICRA. IEEE International Conference on Robotics and Automation (Cat. No.01CH37164), 2002
A model to predict the effect of global and local conformability on grasp static stability is presented. Conformability is defined as the geometric similarity between a workpiece and the smallest polyhedron fit over all contacts. Two conformability metrics, C/sub 1/ and C/sub 2/, that quantify global and local conformability, respectively, are ...
Jose F. Hurtado, Shreyes N. Melkote
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Mutations and the conformational stability of globular proteins

Naturwissenschaften, 1983
The elucidation of the three-dimensional structure of now over 100 proteins provides the basis for describing the nature of interactions stabilizing native protein structure. To understand the forces responsible for maintaining the native structure, it is necessary to analyze the contributions of the specific forces like a hydrogen bond, a salt bridge ...
Grütter, Markus G., Hawkes, Richard B.
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Spermine stabilizes the conformation of tRNAPhe in crystals

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1976
Crystals from yeast tRNAPhe were dissolved and compared with tRNAPhe that had not been srystallized. A number of differences were found regarding the interaction with ethidium bromide, the melting point and the circular dichroic signal. These differences were assigned to the presence of spermine in the dissolved crystals indicating a transient ...
H, Prinz, N, Furgac, F, Cramer
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A Theoretical View on the Conformer Stabilization of Butane

The Journal of Organic Chemistry, 2009
The rotational barrier and conformer energies of butane are well-known, but the contributing effects to its conformational isomerism are still unclear. Calculated potential energy surfaces for the relaxed and vertical (bond distances and angles frozen) structures, together with NBO analysis, suggest that approaching or distancing methyl groups involve ...
Rodrigo A, Cormanich, Matheus P, Freitas
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On stability of classes of conformal mappings. II

Siberian Mathematical Journal, 1995
[For Parts I and II, see Sib. Math. J. 36, No. 2, 305-323 (1995; Zbl 0876.30023) and Sib. Math. J. 38, No. 2, 281-295 (1997; Zbl 0947.30012).] The author studies stability of the class \(\mathfrak G^2\) of mappings defined as follows. Let \(n\) and \(m\) be naturals such that \(n>m\) \((m\geq 2)\).
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Conformational Stabilization of an Engineered Binding Protein

Journal of the American Chemical Society, 2006
We analyzed the thermodynamic basis for improvement of a binding protein by disulfide engineering. The Z(SPA)(-)(1) affibody binds to its Z domain binding partner with a dissociation constant K(d) = 1.6 microM, and previous analyses suggested that the moderate affinity is due to the conformational heterogeneity of free Z(SPA)(-)(1) rather than to a ...
Elisabet, Wahlberg, Torleif, Härd
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Stability of folded conformations

Current Opinion in Structural Biology, 1991
Abstract Significant advances have been made in understanding the thermodynamics of the hydrophobic effect and of the reversible unfolding of proteins, although there is still considerable controversy. Recent analyses suggest that the predominant factor in stabilizing the folded states of proteins is intramolecular hydrogen bonding even though in the
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Conformational stabilization of enzymes in covalent catalysis

Archives of Biochemistry and Biophysics, 1978
Abstract The enzymes aspartate aminotransferase, rhodanese, and chymotrypsin form covalent substituted-enzyme intermediates during the course of their catalysis. The present analyses show that, in these covalent intermediates, the enzyme proteins are stabilized against pH-induced structural transitions to inert forms that occur in the free enzyme ...
M, Volini, S F, Wang
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Forces contributing to the conformational stability of proteins

The FASEB Journal, 1996
For 35 years, the prevailing view has been that the hydrophobic effect is the dominant force in protein folding. The importance of hydrogen bonding was always clear, but whether it made a net favorable contribution to protein stability was not.
C N, Pace, B A, Shirley, M, McNutt, K, Gajiwala   +3 more
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