Results 301 to 310 of about 715,907 (344)
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Conformational interconversion in protein crystals
Journal of Molecular Biology, 1992We 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 +4 more
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Conformation Polymorphism of Polyglutamine Proteins
Trends in Biochemical Sciences, 2018Expanded 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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Conformational stability of globular proteins
Trends in Biochemical Sciences, 1990The conformational stability of ribonuclease T1 has been measured as a function of the variables of most interest to biochemists: temperature, pH, salt concentration, disulfide-bond content and amino acid sequence. The results provide insight into the forces that stabilize globular proteins.
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Conformations of amino acids in proteins
Acta Crystallographica Section D Biological Crystallography, 2002The 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 +2 more
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Characterizing Intermediate Conformations in Protein Conformational Space
2013In this paper we present a novel parallel coordinate based clustering method using Gaussian mixture distribution models to characterize the conformational space of proteins. We detect highly populated regions which may correspond to intermediate states that are difficult to detect experimentally.
Rosanne Vetro +2 more
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Design of protein conformational switches
Current Opinion in Structural Biology, 2006Protein 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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The ABC of protein kinase conformations
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2015Due 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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Conformational Changes in Protein Function
2008Conformational 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 +5 more
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Conformations of disulfide bridges in proteins
International Journal of Peptide and Protein Research, 1990The conformational characteristics of disulfide bridges in proteins have been analyzed using a dataset of 22 protein structures, available at a resolution of 2.0 Å, containing a total of 72 disulfide crosslinks. The parameters used in the analysis include (φ, Ψ) values at Cys residues, bridge dihedral angles χss, χ1i, χ1j, χ2i and χ2j the distances ...
Srinivasan, N +3 more
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Protein conformation in bacterial spinae
Biopolymers, 1976AbstractThe 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 +2 more
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