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Sunday, May 3, 2020 | History

2 edition of Proton exchange behaviour of proteins. found in the catalog.

Proton exchange behaviour of proteins.

Simon Hermanus de Bruin

Proton exchange behaviour of proteins.

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  • 30 Currently reading

Published by Offsetdrukkerij Faculteit der Wiskunde en Natuurwetenschappen (Wilhelminasingel 13) in Nijmegen .
Written in English

    Subjects:
  • Proteins.,
  • Ion exchange.,
  • Chemical equilibrium.,
  • Electric conductivity.

  • Classifications
    LC ClassificationsQD431 .B84
    The Physical Object
    Paginationii, 70 p.
    Number of Pages70
    ID Numbers
    Open LibraryOL4776941M
    LC Control Number75466538

    Proton relaxation times of protein solutions, bovine brain, and edematous feline brain tissue were studied as a function of water concentration, protein concentration, and temperature. In accordance with the fast proton exchange model for relaxation, a linear relation could be established between R1 and the inverse of the weight fraction of.


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Proton exchange behaviour of proteins. by Simon Hermanus de Bruin Download PDF EPUB FB2

The study of the proton exchange of proteins in relationship to their struc­ tural properties. This step was a logical consequence because it appeared Proton exchange behaviour of proteins.

book the study of the latter subject was much facilitated by analysing the differ­ ential titration curve instead of the normal titration curve. This item appears in the following Collection(s) Academic publications [] Academic output Radboud University; Electronic publications [] Freely accessible full text publications plus those not yet available due to embargoAuthor: S.H.

de Bruin. Author(s): Bruin,Simon Hermandus de Title(s): Proton exchange behaviour of proteins/ door Simon Hermanus de Bruin.

Country of Publication: Netherlands Publisher: Nijmegen [Netherlands]: Offsetdrukkerij Faculteit der Wiskunde en Natuurwetenscheppen, [?] Description: 70 p.: ill. Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature.

Heinrich Roder; Gerhard Wagner; Kurt WuethrichCited by: Download PDF: Sorry, we are unable to provide the full text but you may find it at the following location(s): (external link); http Author: S.H. de Bruin. The Protein Book: A Complete Guide for the Athlete and Coach examines the topic of protein nutrition for both endurance and strength/power athletes.

With over pages and referencing over scientific studies, the book will serve as a reference on all aspects of optimal protein nutrition for athletes/5(2). The observed variation among residues in their exchange behavior appears to depend on the structural environment of the side chain.

Understanding this type of exchange process is critical to correctly interpreting NMR spectra of methylated lysine side : Ulrich Weininger, Kristofer Modig, Hiroaki Ishida, Hans J.

Vogel, Mikael Akke. H/D exchange rates of the native protein identified a number of very stable backbone amide protons in the V L and the V H domains. In the V L domain, this slowly exchanging core of the scFv fragment is similar to the folding core of the intermediate, while the V H domain possesses a great number of very stable amide protons which are not stabilized to a significant degree in Cited by: We Proton exchange behaviour of proteins.

book analyzed the pH dependencies of published amide proton exchange rates (kex) in three proteins: bovine pancreatic trypsin inhibitor (BPTI), bull seminal plasma proteinase inhibitor IIA (BUSI IIA), and calbindin by: Analysis of proton exchange kinetics with time-dependent exchange rate.

Since this behavior is observed for protein in the native state in the absence of any denaturant (like urea or high temperature) it proves that the hydrogen exchange in lysozyme occurs by local fluctuation. The latter allows Proton exchange behaviour of proteins. book molecules to penetrate the protein Cited by: 2.

These protein complexes are numbered as I, III, and IV and are known as the Proton exchange behaviour of proteins. book membrane proteins. Explanation of Solution The proton pump transfers the protons or the hydrogen ions from the matrix towards the intermembrane compartment, which elevates the proton Proton exchange behaviour of proteins.

book inside the membrane. Slow exchange lifetimes (from minutes to days) are determined by following the loss of amide proton signal intensity of a protein dissolved in D 2 O, and provide information about relative solvent Cited by:   Partially Fluorinated Polyphenylene Ionomers as Proton Exchange Membranes Proton exchange behaviour of proteins.

book Fuel Cells: Effect of Pendant Multi-Sulfophenylene Groups Zhi Long Interdisciplinary Graduate School of Medicine and Engineering, University of Yamanashi, 4 Author: Zhi Long, Junpei Miyake, Kenji Miyatake.

The gathering of data on the function of membrane proteins prior to knowledge of their structure is valuable for characterizing and defining the proteins. Once the structure is known, another stage of research will penetrate to the functional assignments of the structure.

We have developed for fuel cells a novel proton exchange membrane (PEM) using inorganic phosphotungstic acid (HPW) as proton carrier and mesoporous silica as matrix (HPW-meso-silica).

The proton conductivity measured by electrochemical impedance spectroscopy is S cm–1 at 90 °C and % relative humidity (RH) with a low activation energy of ∼14 kJ mol– by: Since the functional behavior of hemoglobin is closely related to its structure, Hb A2 has been the subject of several studies These studies have all presented evidence that in the region between pH and the Bohr effect, i.e.

the mutual dependence of the oxygen and proton affinity of hemoglobin, is the same for both by: The charge on the protein affects its behavior in ion exchange chromatography.

Proteins contain many ionizable groups on the side chains of their amino acids including their amino - and carboxyl - termini. Chemistry of hydrogen exchange. The exchangeable hydrogens of proteins include the main-chain peptide group NH and the side-chain protons bound to N, O and S atoms of polar groups.

In nucleic acids, the ring imino NHs and the exocyclic amino group (NH 2) protons show facile by: The assigned exchangeable proton signals in the proton nuclear magnetic resonance spectra of sperm whale deoxy and Met-cyano myoglobin in H2O solution were found to exhibit pH-dependent saturation transfer from the bulk water, which allowed determination of the kinetics and mechanism of the labile proton exchange with by: Protein hydrogen atoms can be grouped according to their H/D-Ex behavior.

The first group of hydrogens exhibit very rapid exchange, and they include hydrogens from side chains containing –OH, –SH, –NH 2, –COOH, and –CONH 2 groups and hydrogens from the amino and carboxy termini.

The exchange rates between these side chains and solvent are too fast for the real Cited by: A proton-exchange membrane, or polymer-electrolyte membrane (PEM), is a semipermeable membrane generally made from ionomers and designed to conduct protons while acting as an electronic insulator and reactant barrier, e.g.

to oxygen and hydrogen gas. This is their essential function when incorporated into a membrane electrode assembly (MEA) of a proton-exchange. The relaxation in protein solutions has mainly been studied by nuclear magnetic relaxation dispersion (NMRD) techniques. NMRD data have mostly been analyzed in terms of fast chemical exchange.

The human voltage-gated proton channel [Hv1(1) or VSDO(2)] plays an important role in the human innate immune system. Its structure differs considerably from those of other cation channels.

It is built solely of a voltage-sensing domain and thus lacks the central pore domain, which is essential for other cation channels. Here, we determined the solution structure of an Cited by: 2. Here we show that these two mainly endosomal CLC proteins instead function as electrogenic Cl-/H+ exchangers (also called antiporters), resembling the transport activity of the bacterial protein Cited by: Gu W, Helms V () Tightly connected water wires facilitate fast proton uptake at the proton entrance of proton pumping proteins.

J Am Chem Soc. ity of proton-exchange membranes based on the dusty-fluid model f ounded on the generalized Stefan-Maxwell equations and including dif fusion and convection, the latter r. If protein exchange from the particles is very slow, with a residence time several times longer than the separation time, one fraction of the protein would elute with the particles and one at the same position as for protein injected alone.

If the exchange is very fast, the protein would elute at the same position as without by: All proteins or polypeptides are a series of linked amino acids. A typical α amino acid consists of a central carbon (which is the alpha carbon in this case) that is attached to an amino group (-NH2), a carboxylic acid (-COOH), a hydrogen atom, and a distinctive R group.

Proton exchange membranes (PEMs) are a key component of a proton exchange membrane fuel cell. Sulfonated polyimides (SPIs) were doped by protic ionic liquid (PIL) to prepare composite PEMs with substantially improved conductivity.

SPIs were synthesized from diamine, 2,2-bis[4-(4-amino-phenoxy)phenyl]propane (BAPP), sulfonated diamine, 4,4'-diamino diphenyl ether-2,2' Cited by: Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a spectroscopic technique to observe local magnetic fields around atomic sample is placed in a magnetic field and the NMR signal is produced by excitation of the nuclei sample with radio waves into nuclear magnetic resonance.

Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR Article in Protein Science 4(4) April with 52 Reads.

Much progress has been made in our understanding of water molecule reactions on surfaces1, proton solvation in gas-phase water clusters2,3 and proton transfer through liquids4.

Compared with our Cited by: Proton exchange membrane fuel cells are clean and efficient energy converters. Their accessible power ranges allow their use in the field of transport or stationary : Vladimir Vishnyakov.

Nuclear magnetic resonance spectroscopy of proteins (usually abbreviated protein NMR) is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes.

Here we show that ovarian cancer G-protein-coupled receptor 1 (OGR1), previously described as a receptor for sphingosylphosphorylcholine 3, acts as a proton-sensing receptor stimulating inositol Cited by: Protein Purification by Ion-Exchange Chromatography.

Ion exchange protein purification is possible because most proteins bear nonzero net electrostatic charges at all pHs except at pH=pI (isoelectric point). At a pH >pI of a given protein, that protein becomes negatively charged (an anion), at the pHprotein, it becomes.

The exchange rates are base catalyzed for both protein forms, with the rate eight times faster in Met-cyano than in deoxy myoglobin. The exchange rate is taken as a measure of the magnitude of the fluctuation in the protein conformation near the heme by: Proton, carbon, nitrogen by either one- or multi-dimensional NMR experiments, chemical shifts, scalar coupling constants, dipolar coupling constants, and NOE-through space connections of free or protein-bound carbohydrates comprise Cited by: 7.

Hydrogen–deuterium exchange (also called H–D or H/D exchange) is a chemical reaction in which a covalently bonded hydrogen atom is replaced by a deuterium atom, or vice versa. It can be applied most easily to exchangeable protons and deuterons, where such a transformation occurs in the presence of a suitable deuterium source, without any catalyst.

The heteronuclear single quantum coherence or heteronuclear single quantum correlation experiment, normally abbreviated as HSQC, is used frequently in NMR spectroscopy of organic molecules and is of particular significance in the field of protein experiment was first described by Geoffrey Bodenhausen and D.

Ruben in The resulting spectrum is two. The pdf behavior of vitamin-B 6 compounds, hydration and proton transfer. FEBS Lett. 5, – () PubMed CrossRef Google Scholar AHRENS, M.-L., MAASS, G., SCHUSTER, P., WINKLER, H.: Kinetic study of the hydration mechanism of vitamin B Cited by: 9.

This proton-powered turbine is predicted to consist of 12 subunits2,3,4, based on data for Escherichia coli5. The yeast mitochondrial enzyme, however, has only 10 by: The hydrogen-deuterium exchange ebook of the indole NH proton Trp were studied at ebook pH values at 25/sup 0/C by /sup 1/H nuclear magnetic resonance.

Exchange rates were approximately first order in hydroxyl ion dependence above pH 8, were relatively independent of pH between pH 7 and 8, and decreased below pH 7.