Results 31 to 40 of about 317,356 (295)

Effect of bet missense mutations on bromodomain function, inhibitor binding and stability [PDF]

, 2016
Lysine acetylation is an important epigenetic mark regulating gene transcription and chromatin structure. Acetylated lysine residues are specifically recognized by bromodomains, small protein interaction modules that read these modification in a ...
Alessandra, Pasquo, Chiaraluce, Roberta, Consalvi, Valerio, Cynthia, Tallant, Lori, Clorinda, Lori, Laura, Petrosino, Maria, Stefan, Knapp   +7 more
core   +2 more sources

Les mécanismes de repliement des protéines solubles [PDF]

Biotechnologie, Agronomie, Société et Environnement, 2000
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  

Human growth hormone inclusion bodies present native-like secondary and tertiary structures which can be preserved by mild solubilization for refolding

Microbial Cell Factories, 2022
Background Native-like secondary structures and biological activity have been described for proteins in inclusion bodies (IBs). Tertiary structure analysis, however, is hampered due to the necessity of mild solubilization conditions.
Rosa Maria Chura-Chambi, Chuck Shaker Farah, Ligia Morganti   +2 more
doaj   +1 more source

Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]

, 2006
During pathogenesis of transmissible spongiform encephalopathies (TSEs) an abnormal form (PrPSc) of the host encoded prion protein (PrPC) accumulates in insoluble fibrils and plaques. The two forms of PrP appear to have identical covalent structures, but
Andrew C. Gill, Ansari AA, Atvinder K. Rullay, Bertozzi CR, Blanch EW, Borchelt D, Caughey B, Caughey B, Caughey B, Caughey BW, Critchley P, David H. Crout, Eberl H, Ferris A, Georges C, Gill AC, Govaerts C, Haire LF, Harris DA, Hornemann S, Ian D. Sylvester, Imanpreet K. Bath, Kazlauskaite J, Kazlauskaite J, Kenyon GL, King SA, Kirby L, Klein TR, Kocienski PJ, Legname G, Matthew R. Hicks, Mui B, Nosjean O, Pan KM, Poss AJ, Safar J, Seddon AM, Shyng SL, Stahl N, Stahl N, Teresa J. T. Pinheiro, Whitesell JK, Wuthrich K, Zahn R, Zhang ZY   +44 more
core   +1 more source

A systematic structural comparison of all solved small proteins deposited in PDB. The effect of disulfide bonds in protein fold

Computational and Structural Biotechnology Journal, 2021
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, Fabio C.L. Almeida, Tatiana Domitrovic, Fernando L. Palhano   +3 more
doaj   +1 more source

NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra Naja naja atra [PDF]

, 2013
The Taiwan cobra (Naja naja atra) chymotrypsin inhibitor (NACI) consists of 57 amino acids and is related to other Kunitz-type inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and Bungarus fasciatus fraction IX (BF9), another chymotrypsin ...
Chang, Long-Sen, Güntert, Peter, Ikeya, Teppei, Lin, Yi-Jan   +3 more
core   +2 more sources

Crystal structure of domain of unknown function 507 (DUF507) reveals a new protein fold

Scientific Reports, 2023
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, Jianlin Cheng, John J. Tanner   +2 more
doaj   +1 more source

Protein Tertiary Structure by Crosslinking/Mass Spectrometry [PDF]

Trends in Biochemical Sciences, 2018
Observing the structures of proteins within the cell and tracking structural changes under different cellular conditions are the ultimate challenges for structural biology. This, however, requires an experimental technique that can generate sufficient data for structure determination and is applicable in the native environment of proteins. Crosslinking/
Michael Schneider, Adam Belsom, Juri Rappsilber   +2 more
openaire   +3 more sources

Why Do Proteins Look Like Proteins?

, 1996
Protein structures in nature often exhibit a high degree of regularity (secondary structures, tertiary symmetries, etc.) absent in random compact conformations.
Helling, Robert, Li, Hao, Tang, Chao, Wingreen, Ned   +3 more
core   +1 more source

Molecular Basis and Consequences of the Cytochrome c-tRNA Interaction. [PDF]

, 2016
The intrinsic apoptosis pathway occurs through the release of mitochondrial cytochrome c to the cytosol, where it promotes activation of the caspase family of proteases.
Christian, Thomas, Hou, Ya-Ming, Liu, Cuiping, Stonestrom, Aaron J, Takase, Ryuichi, Yang, Xiaolu, Yong, Jeongsik   +6 more
core   +2 more sources