Results 31 to 40 of about 168,206 (155)
Les mécanismes de repliement des protéines solubles [PDF]
Mechanisms of folding of soluble proteins. The function of a protein is carried out by its three-dimensional structure. The rules for translation of the information encoded by DNAinto an amino acid sequence are well known.
Brasseur B., Benhabilès N., Thomas A.
doaj
Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein
A tertiary structure governs, to a great extent, the biological activity of a protein in the living cell and is consequently a central focus of numerous studies aiming to shed light on cellular processes central to human health. Here, we aim to elucidate
Gideon K. Gogovi +5 more
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Defensins are small proteins, usually ranging from 3 to 6 kDa, amphipathic, disulfide-rich, and with a small or even absent hydrophobic core. Since a hydrophobic core is generally found in globular proteins that fold in an aqueous solvent, the peculiar ...
Mariana H. Moreira +3 more
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Crystal structure of domain of unknown function 507 (DUF507) reveals a new protein fold
The crystal structure of the domain of unknown function family 507 protein from Aquifex aeolicus is reported (AaDUF507, UniProt O67633, 183 residues). The structure was determined in two space groups (C2221 and P3221) at 1.9 Å resolution.
Cole E. McKay +2 more
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PROTINFO: secondary and tertiary protein structure prediction [PDF]
Information about the secondary and tertiary structure of a protein sequence can greatly assist biologists in the generation and testing of hypotheses, as well as design of experiments. The PROTINFO server enables users to submit a protein sequence and request a prediction of the three-dimensional (tertiary) structure based on comparative modeling ...
Ling-Hong, Hung, Ram, Samudrala
openaire +2 more sources
Prediction of Protein Tertiary Structures Using MUFOLD [PDF]
There have been steady improvements in protein structure prediction during the past two decades. However, current methods are still far from consistently predicting structural models accurately with computing power accessible to common users. To address this challenge, we developed MUFOLD, a hybrid method of using whole and partial template information
Jingfen, Zhang +6 more
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Multiple co-evolutionary networks are supported by the common tertiary scaffold of the LacI/GalR proteins. [PDF]
Protein families might evolve paralogous functions on their common tertiary scaffold in two ways. First, the locations of functionally-important sites might be "hard-wired" into the structure, with novel functions evolved by altering the amino acid (e.g.
Daniel J Parente, Liskin Swint-Kruse
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RNA biogenesis and mRNA transport are an intricate process for every eukaryotic cell. SAGA, a transcriptional coactivator and TREX-2 are the two major complexes participate in this process.
Akhilendra Pratap Bharati +4 more
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Protein structure alignment algorithms are often time-consuming, resulting in challenges for large-scale protein structure similarity-based retrieval.
Chunqiu Xia +4 more
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Protein structure prediction is a challenge. A new deep learning framework, CopulaNet, is a major step forward toward end-to-end prediction of inter-residue distances and protein tertiary structures with improved accuracy and efficiency.
Fusong Ju +6 more
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