Results 331 to 340 of about 2,385,840 (355)

Modeling side-chain conformation

Current Opinion in Structural Biology, 1996
Over the past few years, a number of methods for the calculation of side-chain conformations in proteins have been described. More recent studies have considered the effect of combinatorial packing, derivations from idealized rotameric structures and, to a limited extent, backbone flexibility on the quality and efficiency of calculations of protein ...
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Heteroaromatic side-chain analogs of pregabalin

Bioorganic & Medicinal Chemistry Letters, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Po-Wai Yuen, Schelkun Robert Michael, David J. Wustrow, Mark G. Vartanian, Ti-Zhi Su, Jack J. Kinsora   +5 more
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Discretization orders for protein side chains

Journal of Global Optimization, 2014
Proteins are important molecules that are widely studied in biology. Since their three-dimensional conformations can give clues about their function, an optimal methodology for the identification of such conformations has been researched for many years. Experiments of Nuclear Magnetic Resonance (NMR) are able to estimate distances between some pairs of
Costa, Virginia, Mucherino, Antonio, Lavor, Carlile, Cassioli, Andrea, Carvalho, Luiz Mariano, Maculan, Nelson   +5 more
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Mutual orientation of main chains and side chains in nematic liquid-crystalline side-chain polysiloxanes

Macromolecular Chemistry and Physics, 1999
The orientation of main-chain segments of some polysiloxanes containing mesogenic side groups was estimated by 29 Si NMR under high-power proton decoupling. The second-order orientation degree related to the orientation distribution of chemical shift tensors was calculated from the spectra.
Wolfgang Weissflog, Andrea Jacobi, Marion Griebel, Günter Hempel, Detlef Reichert   +4 more
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Synthesis of Paullones with Aminoalkyl Side Chains

Archiv der Pharmazie, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
Daniel W. Zaharevitz, Laurent Meijer, Maryse Leost, Karen Wieking, Conrad Kunick, Marie Knockaert   +5 more
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Motion of Spin-Labeled Side Chains in T4 Lysozyme:  Effect of Side Chain Structure

Biochemistry, 1999
Previous studies have shown that the mobility of nitroxide side chains in a protein, inferred from the electron paramagnetic resonance (EPR) spectra, can be used to classify particular sites as helix surface sites, tertiary contact sites, buried sites, or loop sites.
Wayne L. Hubbell, Tamás Kálai, Hassane S. Mchaourab, Kálmán Hideg   +3 more
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Potent side‐chain to side‐chain cyclized dermorphin analogues containing a carbonyl bridge

Journal of Peptide Science, 2003
AbstractA new family of cyclic opioid peptide analogues related to the 1–4 sequence of dermorphin/deltorphin (Tyr‐D‐Aaa2‐Phe‐Aaa4‐NH2) has been synthesized. The synthesis of the linear precursor peptides was accomplished by the solid‐phase method and ring formation was achieved via a ureido group incorporating the side chain amino functions of D‐Aaa2 ...
Danuta Pawlak, Jan Izdebski, Marta Oleszczuk, Nga N. Chung, Peter W. Schiller, Jacek Wójcik, Katarzyna Filip   +6 more
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Chymotrypsin inhibitory conformation of dipeptides constructed by side chain–side chain hydrophobic interactions

Journal of Molecular Recognition, 1993
AbstractA complete series of configurationally isomers (L‐L, L‐D, D‐L AND D‐D) of a dipeptide Leu‐Phe benzyl ester have been synthesized and assayed for chymotrypsin. In the conformational analysis by 400 MMz 1H NMR, the L‐D and D‐L isomers, but not hte L‐L and D‐D isomers, showed fairly large up field shifts (0.2–0.4 ppm) of Leu‐βCH2 and γCH proton ...
Iori Maeda, Tomoshisa Ogawa, Hiroshi Sakamoto, Keiichi Kawano, Kinichi Nakashima, Yasuyuki Shimohigashi, Takeru Nose, Motonori Ohno, Ichiro Nakamura   +8 more
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Activity profiles of novel side-chain to side-chain cyclized opioid peptide analogs

Neuropeptides, 1984
A new family of opioid peptide analogs cyclized through amide bond formation between side-chain amino and carboxyl groups was tested in mu- and delta-opioid receptor selective bio- and binding assays. Within the series of compounds investigated considerable variation in potency and receptor selectivity was observed as a consequence of the introduced ...
Thi M.-D. Nguyen, Peter W. Schiller
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Environment of tryptophan side chains in proteins

Proteins: Structure, Function, and Genetics, 2000
Although relatively rare, the tryptophan residue (Trp), with its large hydrophobic surface, has a unique role in the folded structure and the binding site of many proteins, and its fluorescence properties make it very useful in studying the structures and dynamics of protein molecules in solution.
Pinak Chakrabarti, Debnath Pal, Uttamkumar Samanta   +2 more
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