نتایج جستجو برای: alpha helix

تعداد نتایج: 224272  

Journal: :Cell 2000
Motoshi Suzuki Richard J. Youle Nico Tjandra

Apoptosis is stimulated by the insertion of Bax from the cytosol into mitochondrial membranes. The solution structure of Bax, including the putative transmembrane domain at the C terminus, was determined in order to understand the regulation of its subcellular location. Bax consists of 9 alpha helices where the assembly of helices alpha1 through alpha 8 resembles that of the apoptosis inhibitor...

2007
J. E. CLUSKEY

The influence of various solvents upon the conformation of gluten proteins, glutenin and gliadin, has been studied by optical rotatory dispersion (ORD), circular dichroism (CD), and infrared (lR) absorption measurements. From ORD data an alpha-helix content of 38% has been calculated for gliadin in trifluoroethanol; 35% for glutenin. Conversely, little or no alpha-helix was found when the prote...

Journal: :Virology 2003
April D Burch Bentley A Fane

Putative conformational switching and inhibitory regions in the Microviridae external scaffolding protein were investigated. Substitutions for glycine 61, hypothesized to promote a postdimerization conformational switch, have dominant lethal phenotypes. In previous studies, chimeric alpha3/phiX174 proteins for structures alpha-helix 1 and loop 6/alpha-helix 7 inhibited phiX174 morphogenesis whe...

Journal: :Biophysical journal 2003
Richard A Dluhy Saratchandra Shanmukh J Brian Leapard Peter Krüger John E Baatz

Bovine pulmonary surfactant protein C (SP-C) is a hydrophobic, alpha-helical membrane-associated lipoprotein in which cysteines C4 and C5 are acylated with palmitoyl chains. Recently, it has been found that the alpha-helix form of SP-C is metastable, and under certain circumstances may transform from an alpha-helix to a beta-strand conformation that resembles amyloid fibrils. This transformatio...

Journal: :The Journal of biological chemistry 2005
Xiaoyong Bao Yongyue Chen Sung Haeng Lee Sung Chang Lee Luis Reuss Guillermo A Altenberg

Approximately 25% of all genome coding sequences correspond to membrane proteins, which perform varied and essential functions in cells. Eukaryotic integral membrane proteins are predominantly alpha-helical proteins that span the membrane several times. The most frequent approach to identifying transmembrane-helix amino acids essential for function is to substitute native residues, one at a tim...

Journal: :Antimicrobial agents and chemotherapy 1999
T Lu X Zhao K Drlica

Antibacterial activities of gatifloxacin (AM1155), a new C-8-methoxy fluoroquinolone, and two structurally related compounds, AM1121 and ciprofloxacin, were studied with an isogenic set of ten quinolone-resistant, gyrA (gyrase) mutants of Escherichia coli. To compare the effect of each mutation on resistance, the mutant responses were normalized to those of wild-type cells. Alleles exhibiting t...

Journal: :Journal of biomolecular NMR 1996
G L Millhauser C J Stenland K A Bolin F J van de Ven

Alanine-rich peptides serve as models for exploring the factors that control helix structure in peptides and proteins. Scalar C alpha H-NH couplings (3JHN alpha) are an extremely useful measure of local helix content; however, the large alanine content in these peptides leads to significant signal overlap in the C alpha H region of 1H 2D NMR spectra. Quantitative determination of all possible 3...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2003
Joel T Welch William R Kearney Sonya J Franklin

A designed lanthanide-binding chimeric peptide based on the strikingly similar geometries of the EF-hand and helix-turn-helix (HTH) motifs was investigated by NMR and CD spectroscopy and found to retain the same overall solution structure of the parental motifs. CD spectroscopy showed that the 33-mer peptide P3W folds on binding lanthanides, with an increase in alpha-helicity from 20% in the ab...

Journal: :Protein engineering 2002
Rudresh Rinku Jain Vardhan Dani Ashima Mitra Sarika Srivastava Siddhartha P Sarma R Varadarajan S Ramakumar

While it is well known that introduction of Pro residues into the interior of protein alpha-helices is destabilizing, there have been few studies that have examined the structural and thermodynamic effects of the replacement of a Pro residue in the interior of a protein alpha-helix. We have previously reported an increase in stability in the P40S mutant of Escherichia coli thioredoxin of 1-1.5 ...

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