Modular design of synthetic protein mimics. Characterization of the helical conformation of a 13-residue peptide in crystals

Biochemistry ◽  
1989 ◽  
Vol 28 (16) ◽  
pp. 6696-6701 ◽  
Author(s):  
Isabella L. Karle ◽  
Judith L. Flippen-Anderson ◽  
K. Uma ◽  
P. Balaram
Keyword(s):  
Modular Design ◽  
Helical Conformation ◽  
Protein Mimics ◽  
Synthetic Protein

Modular design of synthetic protein mimics. Crystal structures, assembly, and hydration of two 15- and 16-residue apolar, leucyl-rich helical peptides

1990 ◽  
Vol 112 (25) ◽  
pp. 9350-9356 ◽  
Author(s):  
Isabella L. Karle ◽  
Judith L. Flippen-Anderson ◽  
K. Uma ◽  
M. Sukumar ◽  
P. Balaram
Keyword(s):  
Crystal Structures ◽  
Modular Design ◽  
Helical Peptides ◽  
Protein Mimics ◽  
Synthetic Protein

Modular design of synthetic protein mimics. Crystal structure of two seven-residue helical peptide segments linked by .epsilon.-aminocaproic acid

1991 ◽  
Vol 113 (10) ◽  
pp. 3952-3956 ◽  
Author(s):  
Isabella L. Karle ◽  
Judith L. Flippen-Anderson ◽  
M. Sukumar ◽  
K. Uma ◽  
P. Balaram
Keyword(s):  
Crystal Structure ◽  
Modular Design ◽  
Aminocaproic Acid ◽  
Protein Mimics ◽  
Synthetic Protein ◽  
Helical Peptide ◽  
Epsilon Aminocaproic Acid ◽  
Peptide Segments

Preparation and Characterization of a Novel Flame Retardant

2008 ◽  
Vol 47-50 ◽  
pp. 294-297 ◽  
Author(s):  
Xiu Wei Jia ◽  
Min Zhi Rong ◽  
Ming Qiu Zhang
Keyword(s):  
Flame Retardant ◽  
Sol Gel ◽  
Average Molecular Weight ◽  
Regular Structure ◽  
Gel Permeation Chromatography ◽  
Helical Conformation ◽  
Infrared Spectrometry ◽  
Resonance Spectroscopy ◽  
X Ray Diffraction

A novel flame retardant polymethylsilsesquioxane (PMSQ) was successfully obtained via combination of non-hydrolytic and hydrolytic sol-gel routes. Chemical structure of the resultant PMSQ was determined by nuclear magnetic resonance spectroscopy, Fourier-transform infrared spectrometry and powder X-ray diffraction, respectively. All the measurements demonstrated that the product possessed regular structure with chain-to-chain width of 0.87nm and chain thickness of 0.40nm. Weight average molecular weight of PMSQ was measured to be 3.5×105 using gel permeation chromatography. Numerical simulations of the molecular structure suggested that PMSQ should exhibit cis-isotactic configuration and double helical conformation at undisturbed condition.

scholarly journals Pushing the limits of automatic computational protein design: design, expression, and characterization of a large synthetic protein based on a fungal laccase scaffold

2011 ◽  
Vol 5 (1-2) ◽  
pp. 45-58 ◽  
Author(s):  
Doris J. Glykys ◽  
Géza R. Szilvay ◽  
Pablo Tortosa ◽  
María Suárez Diez ◽  
Alfonso Jaramillo ◽  
...  
Keyword(s):  
Protein Design ◽  
Computational Protein Design ◽  
Fungal Laccase ◽  
Synthetic Protein

scholarly journals Characterization of Endolysin LyJH307 with Antimicrobial Activity against Streptococcus bovis

Animals ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 963 ◽  
Author(s):  
Hanbeen Kim ◽  
Hyo Gun Lee ◽  
Inhyuk Kwon ◽  
Jakyeom Seo
Keyword(s):  
Metal Ion ◽  
Modular Design ◽  
Ethylenediaminetetraacetic Acid ◽  
Streptococcus Bovis ◽  
Cell Wall Binding ◽  
Zoocin A ◽  
Alkaline Conditions ◽  
A Cell ◽  
Cell Wall Binding Domain

Streptococcus bovis (S. bovis) is one of the critical initiators of acute acidosis in ruminants. Therefore, we aimed to develop and characterize the endolysin LyJH307, which can lyse ruminal S. bovis. We tested the bactericidal activity of recombinant LyJH307 against S. bovis JB1 under a range of pH, temperature, NaCl, and metal ion concentrations. In silico analyses showed that LyJH307 has a modular design with a distinct, enzymatically active domain of the NLPC/P60 superfamily at the N-terminal and a cell wall binding domain of the Zoocin A target recognition domain (Zoocin A_TRD) superfamily at the C-terminal. The lytic activity of LyJH307 against S. bovis JB1 was the highest at pH 5.5, and relatively higher under acidic, than under alkaline conditions. LyJH307 activity was also the highest at 39 °C, but was maintained between 25°C and 55°C. LyJH307 bactericidal action was retained under 0-500 mM NaCl. While the activity of LyJH307 significantly decreased on treatment with ethylenediaminetetraacetic acid (EDTA), it was only restored with supplementation of 10 mM Ca2+. Analyses of antimicrobial spectra showed that LyJH307 lysed Lancefield groups D (S. bovis group and Enterococcus faecalis) and H (S. sanguinis) bacteria. Thus, LyJH307 might help to prevent acute ruminal acidosis.

scholarly journals Structural and functional characterization of the pore-forming domain of pinholin S2168

2020 ◽  
Vol 117 (47) ◽  
pp. 29637-29646
Author(s):  
Lena M. E. Steger ◽  
Annika Kohlmeyer ◽  
Parvesh Wadhwani ◽  
Jochen Bürck ◽  
Erik Strandberg ◽  
...  
Keyword(s):  
Experimental Data ◽  
Order Parameter ◽  
Transmembrane Domain ◽  
Functional Characterization ◽  
Azimuthal Angle ◽  
Structural Models ◽  
Lytic Cycle ◽  
Helical Conformation ◽  
Rotational Orientation

Pinholin S2168 triggers the lytic cycle of bacteriophage φ21 in infectedEscherichia coli. Activated transmembrane dimers oligomerize into small holes and uncouple the proton gradient. Transmembrane domain 1 (TMD1) regulates this activity, while TMD2 is postulated to form the actual “pinholes.” Focusing on the TMD2 fragment, we used synchrotron radiation-based circular dichroism to confirm its α-helical conformation and transmembrane alignment. Solid-state15N-NMR in oriented DMPC bilayers yielded a helix tilt angle of τ = 14°, a high order parameter (Smol= 0.9), and revealed the azimuthal angle. The resulting rotational orientation places an extended glycine zipper motif (G40xxxS44xxxG48) together with a patch of H-bonding residues (T51, T54, N55) sideways along TMD2, available for helix–helix interactions. Using fluorescence vesicle leakage assays, we demonstrate that TMD2 forms stable holes with an estimated diameter of 2 nm, as long as the glycine zipper motif remains intact. Based on our experimental data, we suggest structural models for the oligomeric pinhole (right-handed heptameric TMD2 bundle), for the active dimer (right-handed Gly-zipped TMD2/TMD2 dimer), and for the full-length pinholin protein before being triggered (Gly-zipped TMD2/TMD1-TMD1/TMD2 dimer in a line).

scholarly journals Structural and Functional Characterization of RecG Helicase under Dilute and Molecular Crowding Conditions

2012 ◽  
Vol 2012 ◽  
pp. 1-8
Author(s):  
Sarika Saxena ◽  
Satoru Nagatoishi ◽  
Daisuke Miyoshi ◽  
Naoki Sugimoto
Keyword(s):  
Functional Characterization ◽  
Cd Spectroscopy ◽  
Helical Conformation ◽  
Atp Binding ◽  
Molecular Crowding ◽  
Active Structure ◽  
Dna Junctions ◽  
Unique Protein

In an ATP-dependent reaction, theEscherichia coliRecG helicase unwinds DNA junctionsin vitro. We present evidence of a unique protein conformational change in the RecG helicase from anα-helix to aβ-strand upon an ATP binding under dilute conditions using circular dichroism (CD) spectroscopy. In contrast, under molecular crowding conditions, theα-helical conformation was stable even upon an ATP binding. These distinct conformational behaviors were observed to be independent of Na+and Mg2+. Interestingly, CD measurements demonstrated that the spectra of a frayed duplex decreased with increasing of the RecG concentration both under dilute and molecular crowding conditions in the presence of ATP, suggesting that RecG unwound the frayed duplex. Our findings raise the possibility that theα-helix andβ-strand forms of RecG are a preactive and an active structure with the helicase activity, respectively.

scholarly journals Molecular characterization of human stathmin expressed in Escherichia coli: site-directed mutagenesis of two phosphorylatable serines (Ser-25 and Ser-63)

1994 ◽  
Vol 300 (2) ◽  
pp. 331-338 ◽  
Author(s):  
P A Curmi ◽  
A Maucuer ◽  
S Asselin ◽  
M Lecourtois ◽  
A Chaffotte ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Kinase ◽  
Glutamic Acid ◽  
Protein Characterization ◽  
Mitogen Activated Protein Kinase ◽  
Helical Conformation ◽  
In Vitro Mutagenesis ◽  
Native Protein

Stathmin, a probable relay protein possibly integrating multiple intracellular regulatory signals [reviewed in Sobel (1991) Trends Biochem. Sci. 16, 301-305], was expressed in Escherichia coli at levels as high as 20% of total bacterial protein. Characterization of the purified recombinant protein revealed that it had biochemical properties very similar to those of the native protein. It is a good substrate for both cyclic AMP-dependent protein kinase (PKA) and p34cdc2, on the same four sites as the native eukaryotic protein. As shown by m.s., the difference in isoelectric points from the native protein is probably due to the absence of acetylation of the protein produced in bacteria. C.d. studies indicate that stathmin probably contains about 45% of its sequence in an alpha-helical conformation, as also predicted for the sequence between residues 47 and 124 by computer analysis. Replacement of Ser-63 by alanine by in vitro mutagenesis resulted in a ten times less efficient phosphorylation of stathmin by PKA which occurred solely on Ser-16, confirming that Ser-63 is the major target of this kinase. Replacement of Ser-25, the major site phosphorylated by mitogen-activated protein kinase in vitro and in vivo, by the charged amino acid glutamic acid reproduced, in conjunction with the phosphorylation of Ser-16 by PKA, the mobility shift on SDS/polyacrylamide gels induced by the phosphorylation of Ser-25. This result strongly suggests that glutamic acid in position 25 is able to mimic the putative interactions of phosphoserine-25 with phosphoserine-16, as well as the resulting conformational changes that are probably also related to the functional regulation of stathmin.

Synthesis and characterization of 2,3-di-O-alkylated amyloses: Hydrophobic substitution destabilizes helical conformation

Biopolymers ◽  
2003 ◽  
Vol 69 (3) ◽  
pp. 301-310 ◽  
Author(s):  
Hans-Georg Breitinger
Keyword(s):  
Helical Conformation ◽  
Synthesis And Characterization

scholarly journals Characterization of the Modular Design of the Autolysin/Adhesin Aaa from Staphylococcus Aureus

PLoS ONE ◽  
2012 ◽  
Vol 7 (6) ◽  
pp. e40353 ◽  
Author(s):  
Nina Hirschhausen ◽  
Tim Schlesier ◽  
Georg Peters ◽  
Christine Heilmann
Keyword(s):  
Staphylococcus Aureus ◽  
Modular Design
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