Now showing items 11-20 of 166
Control of acetylcholine receptor mobility and distribution in cultured muscle membranes. A fluorescence study
(Elsevier, 1978-07-20)
The molecular control of the distribution and motion of acetylcholine receptors in the plasma membrane of developing rat myotubes in primary cell culture was investigated by fluorescence techniques. Acetylcholine receptors ...
Highly Efficient, Near-Infrared Electrophosphorescence from a Pt–Metalloporphyrin Complex The authors acknowledge financial support from the U.S. Dept. of the Army, CECOM for the phase 14II SBIR program (contract no. 14W15P7T-06-C-T201), and Universal Display Corporation.
(WILEY-VCH Verlag, 2007-02-05)
No Abstract
Normal mode spectrum of the parallel-chain Β-sheet This is paper number 39 in a series on “Vibrational Analysis of Peptides, Polypeptides, and Proteins,” of which paper number 38 is Ref. 19.
(Wiley Subscription Services, Inc., A Wiley Company, 1988-06)
Normal mode calculations have been carried out for parallel-chain Β-sheet structures. These include the parallel-chain pleated sheet of poly( L -alanine) and the parallel-chain rippled sheet of polyglycine. Dipole derivative ...
Conformation-sensitive infrared carbon-chlorine bands of polyvinyl chloride
(John Wiley & Sons, Inc., 1964-11)
No Abstract.
Circular dichroism of the “random” polypeptide chain
(Wiley Subscription Services, Inc., A Wiley Company, 1969-09)
The circular dichroism (CD) spectrum of an unordered polypeptide chain does not correspond, as has been assumed heretofore, to that of a charged chain such as poly- L -glutamic acid or poly- L -lysine. The latter have been ...
Contributions of the nanovoid structure to the kinetics of moisture transport in epoxy resins
(John Wiley & Sons, Inc., 2000-03-01)
Absorbed moisture can degrade the physical properties of an epoxy resin, jeopardizing the performance of an epoxy-based component. Although specific water–epoxy interactions are known to be very important in determining ...
Vibrational analysis of peptides, polypeptides, and proteins. XVIII. Conformational sensitivity of the Α-helix spectrum: Α I - and Α II -Poly( L -alanine)
(Wiley Subscription Services, Inc., A Wiley Company, 1984-05)
The Α II -helix (φ = −70.47°, Ψ = −35.75°) is a structure having the same n and h as the (standard) Α I -helix (φ = −57.37°, Ψ = −47.49°). Its conformational angles are commonly found in proteins. Using an improved ...
The hydrophobic effect: Formation of micelles and biological membranes, Charles Tanford, Wiley-Interscience, New York, 1980, 233 pp. price: $18.50.
(John Wiley & Sons, Inc., 1980-10)
No Abstract.
Ab initio force fields of alanine dipeptide in four non-hydrogen bonded conformations
(Elsevier, 1990-03)
We have previously calculated the force fields and dipole-moment derivatives of the L-alanyl dipeptide, CH3CONHCHCH2CONHCH3, in the C5, C7eq, and C7ax conformations with intramolecular NH...OC hydrogen bonding. We have now ...
A quantitative anharmonic analysis of the amide A band in α-helical poly( L -alanine)
(John Wiley & Sons, Inc., 1999-03)
Polarized ir spectra of oriented films of α-helical poly( l -alanine) (α-PLA) have been obtained as a function of residual solvent dichloroacetic acid (DCA). The amide A, B, II, and V regions exhibit multiple bands whose ...