نتایج جستجو برای: alpha helix

تعداد نتایج: 224272  

Journal: :The Journal of biological chemistry 2004
Albert Carson Harrod Xiaofeng Yang Matthew Junker Larry Reitzer

Nitrogen limitation in Escherichia coli activates about 100 genes. Their expression requires the response regulator NtrC (also called nitrogen regulator I or NR(I)). Phosphorylation of the amino-terminal domain (NTD) of NtrC activates the neighboring central domain and leads to transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. The NTD has five beta stra...

Journal: :Biochimica et biophysica acta 2005
Jesús Mendieta Miguel A Fuertes Rani Kunjishapatham Ismael Santa-María Francisco J Moreno Carlos Alonso Federico Gago Victor Muñoz Jesús Avila Félix Hernández

Paired helical filaments (PHFs) isolated from patients with Alzheimer's disease (AD) mainly consist of the microtubule-associated protein tau in a hyperphosphorylated form. It has been found that PHFs are the first example of pathological protein aggregation associated with formation of alpha-helices [Biochemistry (2002) 41, 7150-5]. In an effort to investigate the interplay between phosphoryla...

Journal: :Chaos Solitons & Fractals 2022

Protein$\alpha$-helices provide an ordered biological environment that is conducive to soliton-assisted energy transport. The nonlinear interaction between amide I excitons and phonon deformations induced in the hydrogen-bonded lattice of peptide groups leads self-trapping energy, thereby creating a localized quasiparticle (soliton) persists at zero temperature. presence thermal noise, however,...

Journal: :European journal of biochemistry 2000
A M Fernández V Villegas J C Martínez N A Van Nuland F Conejero-Lara F X Avilés L Serrano V V Filimonov P L Mateo

Thermodynamic characterization of the activation domain of human procarboxypeptidase A2, ADA2h, and its helix-engineered mutants was carried out by differential scanning calorimetry. The mutants were engineered by changing residues in the exposed face of the two alpha helices in order to increase their stability. At neutral and alkaline pH the three mutants, alpha-helix 1 (M1), alpha-helix 2 (M...

Journal: :Biochemistry 2008
Fujiang Zhu Paul Davies Andrew R Thompsett Sharon M Kelly George E Tranter Lutz Hecht Neil W Isaacs David R Brown Laurence D Barron

The binding of divalent copper ions to the full-length recombinant murine prion protein PrP23-231 at neutral pH was studied using vibrational Raman optical activity (ROA) and ultraviolet circular dichroism (UV CD). The effect of the Cu2+ ions on PrP structure depends on whether they are added after refolding of the protein in water or are present during the refolding process. In the first case ...

Journal: :Biochemistry 2005
Angeliki Chroni Adelina Duka Horng-Yuan Kan Tong Liu Vassilis I Zannis

We have analyzed the effect of charged to neutral amino acid substitutions around the kinks flanking helices 4 and 6 of apoA-I and of the deletion of helix 6 on the in vivo activity of LCAT and the biogenesis of HDL. The LCAT activation capacity of apoA-I in vitro was nearly abolished by the helix 6 point (helix 6P-apoA-I[R160V/H162A]) and deletion {helix 6Delta-apoA-I[Delta(144-165)]} mutants,...

Journal: :Journal of Chemical Education 1984

Journal: :The Journal of Biological Chemistry 2009
Ella R. Hinson Peter Cresswell

Viperin is an evolutionarily conserved interferon-inducible protein that localizes to the endoplasmic reticulum (ER) and inhibits a number of DNA and RNA viruses. In this study, we report that viperin specifically localizes to the cytoplasmic face of the ER and that an amphipathic alpha-helix at its N terminus is necessary for the ER localization of viperin and sufficient to promote ER localiza...

Journal: :Proceedings of the National Academy of Sciences 1992

Journal: :International Journal of Scientific Research in Science, Engineering and Technology 2020

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