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    Academic Journals

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• Cooperativity in protein folding: theory and experiment

  Author:H.S. ChanFrom:Biochemistry and Cell Biology (Vol. 88, Issue 2) Peer-Reviewed

  Apr. 2010220 words Brief article, Repor... Many small single-domain proteins undergo cooperative, switch-like folding/unfolding transitions with very low populations of intermediate (i.e., partially folded) conformations. Contrary to widely held expectations,...

• Does SDS denature membrane proteins? The link between SDS-PAGE migration and membrane protein folding

  Authors:C.M. Deber, V. Nadeau, and A. RathFrom:Biochemistry and Cell Biology (Vol. 88, Issue 2) Peer-Reviewed

  Apr. 2010313 words Brief article, Repor... 1470LMigration on SDS-PAGE that does not correlate with formula molecular masses, termed "gel shifting," appears to be common for membrane proteins. Here, we will discuss the anomalous gel mobility of helical membrane...

• A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids

  Authors:Karyn T. O'Neil and William F. DeGradoFrom:Science (Vol. 250, Issue 4981) Peer-Reviewed

  Nov. 2, 19904,596 words Article Amino acids have distinct conformational preferences that influence the stabilities of protein secondary and tertiary structures. The relative thermodynamic stabilities of each of the 20 commonly occurring amino acids in...

• Detection of transient protein folding populations by mass spectrometry

  Authors:Andrew Miranker, Carol V. Robinson, Sheena E. Radford, Robin T. Aplin, and Christopher M. DobsonFrom:Science (Vol. 262, Issue 5135) Peer-Reviewed

  Nov. 5, 19933,675 words Article Hydrogen-deuterium exchange measurements are becoming increasingly important in studies of the dynamics of protein molecules and, particularly, of their folding behavior. Electrospray ionization mass spectrometry...

• Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A

  Authors:Stephen L. Mayo and Robert L. BaldwinFrom:Science (Vol. 262, Issue 5135) Peer-Reviewed

  Nov. 5, 19933,696 words Article Amide (NH) proton exchange rates were measured in 0.0 to 0.7 M guanidinium chloride (GdmCl) for 23 slowly exchanging peptide NH protons of ribonucleases A (RNase A) at pH* 5.5 (uncorrected pH measured in [D.sub.2]O), 34...

• In pursuit of protein folding

  Author:S. Walter EnglanderFrom:Science (Vol. 262, Issue 5135) Peer-Reviewed

  Nov. 5, 19931,920 words Article Protein folding intermediates have been hard to identify because they last for less than a second, but a new method based on hydrogen exchange, using both regular and heavy water, catches them in process. Research groups...

• Possible exceptions to rules for Alpha-helix termination by glycine

  Authors:Eric L. Altschuler and Martin LadesFrom:Science (Vol. 269, Issue 5229) Peer-Reviewed

  Sept. 8, 19951,613 words Article Possible exceptions are described to rules determining whether a propagating Alpha-helix will terminate or propagate through glycine upon reaching it. If these exceptions cannot be explained, it may not be possible to...

• Direct observation of protein solvation and discrete disorder with experimental crystallographic phases

  Authors:F. Temple Burling, William I. Weis, Kevin M. Flaherty, and Axel T. BrungerFrom:Science (Vol. 271, Issue 5245) Peer-Reviewed

  Jan. 5, 19964,226 words Article A complete and accurate set of experimental crystallographic phases to a resolution of 1.8 angstroms was obtained for a 230-residue dimeric fragment of rat mannose-binding protein A with the use of multiwavelength...

• Guidelines for protein design: the energetics Beta sheet side chain interactions

  Authors:Catherine K. Smith and Lynne ReganFrom:Science (Vol. 270, Issue 5238) Peer-Reviewed

  Nov. 10, 19952,509 words Article To determine the interaction energy between cross-strand pairs of side chains on an antiparallel [beta] sheet, pairwise amino acid substitutions were made on the solvent-exposed face of the B1 domain of streptococcal...

• Mechanism of folding chamber closure in a group II chaperonin

  Authors:Junjie Zhang, Matthew L. Baker, Gunnar F. Schroder, Nicholai R. Douglas, Stefanie Reissmann, Joanita Jakana, et al.From:Nature (Vol. 463, Issue 7279) Peer-Reviewed

  Jan. 21, 20105,163 words Report 1440LGroup II chaperonins are essential mediators of cellular protein folding in eukaryotes and archaea. These oligomeric protein machines, ~1 megadalton, consist of two back-to-back rings encompassing a central cavity that...

• Denaturation properties and folding transition states of leghemoglobin and other heme proteins

  Authors:Pijush Basak, Niloy Kundu, Rudradip Pattanayak, and Maitree BhattacharyyaFrom:Biochemistry (Moscow) (Vol. 80, Issue 4) Peer-Reviewed

  Apr. 20153,136 words Report 1380LThis work reports unfolding transitions of monomeric heme proteins leghemoglobin (Lb), myoglobin (Mb), and cytochrome c (Cyt c) utilizing UV-Vis spectra, steady-state and time-resolved fluorescence methods....

• Evolution of a Protein Fold in Vitro

  Authors:Matthew H. J. Cordes, Nathan P. Walsh, C. James McKnight, and Robert T. SauerFrom:Science (Vol. 284, Issue 5412) Peer-Reviewed

  Apr. 9, 19992,626 words Article A "switch" mutant of the Arc repressor homodimer was constructed by interchanging the sequence positions of a hydrophobic core residue, leucine 12, and an adjacent surface polar residue, asparagine 11, in each strand of...

• Analysis of an immune algorithm for protein structure prediction

  Authors:Andrew J. Bennett, Roy L. Johnston, Eleanor Turpin, and Jun Q. HeFrom:Informatica (Vol. 32, Issue 3) Peer-Reviewed

  Oct. 20082,739 words Report 1530LThe aim of a protein folding simulation is to determine the native state of a protein from its amino acid sequence. In this paper we describe the development and application of an Immune Algorithm (IA) to find the...

• Prion protein misfolding, strains, and neurotoxicity: an update from studies on mammalian prions

  Authors:Ilaria Poggiolini, Daniela Saverioni, and Piero ParchiFrom:International Journal of Cell BiologyPeer-Reviewed

  Annual 201420,497 words Report 1730LPrion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders affecting humans and other mammalian species. The central event in TSE pathogenesis is the...

• Machine Learning: How Much Does It Tell about Protein Folding Rates?

  Authors:Marc Corrales, Pol Cusco, Dinara R. Usmanova, Heng-Chang Chen, Natalya S. Bogatyreva, Guillaume J. Filion, et al.From:PLoS ONE (Vol. 10, Issue 11) Peer-Reviewed

  Nov. 25, 20154,953 words Article 1410LThe prediction of protein folding rates is a necessary step towards understanding the principles of protein folding. Due to the increasing amount of experimental data, numerous protein folding models and predictors of...

• Exploring the Conserved Role of MANF in the Unfolded Protein Response in Drosophila melanogaster

  Authors:Riitta Lindstrom, Paivi Lindholm, Jukka Kallijarvi, Mari Palgi, Mart Saarma, and Tapio I. HeinoFrom:PLoS ONE (Vol. 11, Issue 3) Peer-Reviewed

  Mar. 14, 20168,795 words Report 1350LDisturbances in the homeostasis of endoplasmic reticulum (ER) referred to as ER stress is involved in a variety of human diseases. ER stress activates unfolded protein response (UPR), a cellular mechanism the purpose of...

• N-glycosylation in the protease domain of trypsin-like serine proteases mediates calnexin-assisted protein folding

  Authors:Hao Wang, Shuo Li, Juejin Wang, Shenghan Chen, Xue-Long Sun, and Qingyu WuFrom:eLife (Vol. 7) Peer-Reviewed

  June 11, 201812,892 words Report 1290LTrypsin-like serine proteases are essential in physiological processes. Studies have shown that N-glycans are important for serine protease expression and secretion, but the underlying mechanisms are poorly understood....

• An effective all-atom potential for proteins

  Authors:Anders Irback, Simon Mitternacht, and Sandipan MohantyFrom:PMC Biophysics (Vol. 2, Issue 2) Peer-Reviewed

  Apr. 8, 20098,343 words Report We describe and test an implicit solvent all-atom potential for simulations of protein folding and aggregation. The potential is developed through studies of structural and thermodynamic properties of 17 peptides with...

• Proteinopathy-induced neuronal senescence: a hypothesis for brain failure in Alzheimer's and other neurodegenerative diseases

  Authors:Todd E Golde and Victor M MillerFrom:Alzheimer's Research & Therapy (Vol. 1, Issue 6) Peer-Reviewed

  Oct. 13, 20099,754 words Report 1500LBackground Alzheimer's disease (AD) and a host of other neurodegenerative central nervous system (CNS) proteinopathies are characterized by the accumulation of misfolded protein aggregates. Simplistically, these...

• A new understanding of protein mutation unfolds: long believed to be nonfunctional mutant proteins that cause disease can often behave normally when refolded with the help of a pharmacological template

  Authors:P. Michael Conn and Jo Ann JanovickFrom:American Scientist (Vol. 93, Issue 4)

  July-August 20054,217 words Article Many diseases are caused by mutations in a person's DNA, since these errors often change the amino acid composition of proteins encoded by genes. Scientists who study genetic diseases frequently experiment on cells that...