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Journal Issue - Volume 11 Issue 8 (August 2002)

Abstract Bombyx mori silk fibroin is a fibrous protein whose fiber is extremely strong and tough, although it is produced by the silkworm at room temperature and from an aqueous solution. The primary structure is mainly Ala‐Gly alternative copolypeptide, but Gly‐Ala‐Ala‐Ser units appear frequently and periodically. Thus, this study aims at elucidating the role of such Gly‐Ala‐Ala‐Ser units on the secondary structure. The sequential...

  • Docking of protein models

  • Andrei Tovchigrechko, Christopher A. Wells, Ilya A. Vakser
  • Published in Wiley Interscience on Jan 01, 2009
  • DOI: 10.1110/ps.4730102 (p 1888-1896)

Abstract An adequate description of entire genomes has to include information on the three‐dimensional (3D) structure of proteins. Most of these protein structures will be determined by high‐throughput modeling procedures. Thus, a structure‐based analysis of the network of protein–protein interactions in genomes requires docking methodologies that are capable of dealing with significant structural inaccuracies in the modeled...

Abstract A complex pathway involving many molecular chaperones has been proposed for the folding, assembly, and maintenance of a high‐affinity ligand‐binding form of steroid receptors in vivo, including the glucocorticoid receptor. To better understand this intricate folding and assembly process, we studied the folding of the ligand‐binding domain of the glucocorticoid receptor in vitro. We found that this domain can be refolded...

Abstract Although much of the motivation for experimental studies of protein folding is to obtain insights for improving protein structure prediction, there has been relatively little connection between experimental protein folding studies and computational structural prediction work in recent years. In the present study, we show that the relationship between protein folding rates and the contact order (CO) of the native structure...

Abstract A monomeric form of acetylcholinesterase from the venom of Bungarus fasciatus is converted to a partially unfolded molten globule species by thermal inactivation, and subsequently aggregates rapidly. To separate the kinetics of unfolding from those of aggregation, single molecules of the monomeric enzyme were encapsulated in reverse micelles of Brij 30 in 2,2,4‐trimethylpentane, or in large unilamellar vesicles of egg...

Abstract Phenylalanine hydroxylase (PAH) is activated by its substrate phenylalanine, and through phosphorylation by cAMP‐dependent protein kinase at Ser16 in the N‐terminal autoregulatory sequence of the enzyme. The crystal structures of phosphorylated and unphosphorylated forms of the enzyme showed that, in the absence of phenylalanine, in both cases the N‐terminal 18 residues including the phosphorylation site contained no...

Abstract The ability of several naturally occurring substances known as osmolytes to induce helix formation in an alanine‐based peptide have been investigated. As predicted by the osmophobic effect hypothesis, the osmolytes studies here do induce helix formation. Trimethylamine‐N‐oxide (TMAO) is the best structure‐inducing osmolytes investigated here, but it is not as effective in promoting helix formation as the common cosolvent...

Abstract The type A γ‐aminobutyric acid (GABAA) receptor is a major inhibitory neurotransmitter‐gated ion channel. Previously, we identified a membrane‐proximal β‐rich (MPBR) domain in fragment C166‐L296 of GABAA receptor α1 subunit, forming nativelike pentamers. In the present study, another structural domain, the amino‐terminal domain, was shown to exist in the fragment Q28‐E165. The secondary structures of both fragments were β‐rich as...