Results 281 to 290 of about 3,930,063 (310)

Conformations of amino acids in proteins

Acta Crystallographica Section D Biological Crystallography, 2002
The main-chain conformations of 237 384 amino acids in 1042 protein subunits from the PDB were analyzed with Ramachandran plots. The populated areas of the empirical Ramachandran plot differed markedly from the classical plot in all regions. All amino acids in alpha-helices are found within a very narrow range of phi, psi angles.
Sven, Hovmöller, Tuping, Zhou, Tomas, Ohlson   +2 more
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Design of protein conformational switches

Current Opinion in Structural Biology, 2006
Protein conformational switches are ubiquitous in nature and often regulate key biological processes. To design new proteins that can switch conformation, protein designers have focused on the two key components of protein switches: the amino acid sequence must be compatible with the multiple target states and there must be a mechanism for perturbing ...
Xavier I, Ambroggio, Brian, Kuhlman
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Conformational mobility of immobilized proteins

Journal of Pharmaceutical and Biomedical Analysis, 2007
Cellular membrane fragments have been immobilized on the surface of a silica-based liquid chromatographic support and on the surface of glass capillaries to create immobilized receptor and drug transporter columns. These columns have included phases containing one subtype of the nicotinic receptor (alpha3beta2, alpha3beta4, alpha4beta2, alpha4beta4 ...
Ruin, Moaddel, Irving W, Wainer
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Protein conformation in bacterial spinae

Biopolymers, 1976
AbstractThe far uv circular dichroism (CD) and infrared spectra of bacterial spinae are reported. Estimates of the protein secondary structure were obtained by three‐component curve‐fitting methods supplemented by rank and factor analysis of CD data matrices. Native spinae were shown to contain approximately 88% antiparallel β‐sheet, 7% α‐helix, and 5%
R W, Coombs, J A, Verpoorte, K B, Easterbrook   +2 more
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The ABC of protein kinase conformations

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2015
Due to their involvement in human diseases, protein kinases are an important therapeutic target class. Conformation is a key concept for understanding how functional activity, inhibition and sequence are linked. We assemble and annotate the mammalian structural kinome from the Protein Data Bank on the basis of a universal residue nomenclature.
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Conformation of terminal regions in proteins

Nature, 1982
A carboxy-terminal helix has been observed in many proteins, suggesting that these helices confer an advantage, perhaps by providing protection against carboxypeptidase activity. To determine whether the conformational preferences of the amino- and carboxy-terminal regions are significantly different from each other and from the rest of the protein, we
J M, Thornton, B L, Chakauya
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Conformational interconversion in protein crystals

Journal of Molecular Biology, 1992
We present evidence that the structure of carbonmonoxy myoglobin crystals can be altered by lowering the pH. This structural change is monitored by the characteristic Fe-CO Raman modes at 508 and 491 cm-1 and is thought to involve a localized distal pocket transition from a "closed" conformation at pH 7 to a more "open" conformation at pH 4.
L, Zhu, J T, Sage, A A, Rigos, D, Morikis, P M, Champion   +4 more
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Conformation Polymorphism of Polyglutamine Proteins

Trends in Biochemical Sciences, 2018
Expanded polyglutamine (polyQ) stretches within endogenous proteins cause at least nine human diseases. The structural basis of polyQ pathogenesis is the key to understanding fundamental mechanisms of these diseases, but it remains unclear and controversial due to a lack of polyQ protein structures at the single-atom level. Various hypotheses have been
Xinran Feng, Shouqing Luo, Boxun Lu
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Conformation of Proteins

Annual Review of Biochemistry, 1967
S N, Timasheff, M J, Gorbunoff
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Conformational Changes in Protein Function

2008
Conformational changes are the hallmarks of protein dynamics and are often intimately related to protein functions. Molecular dynamics (MD) simulation is a powerful tool to study the time-resolved properties of protein structure in atomic details.
Haiguang, Liu, Shubhra Ghosh, Dastidar, Hongxing, Lei, Wei, Zhang, Matthew C, Lee, Yong, Duan   +5 more
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