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Wyszukujesz frazę "molten globule" wg kryterium: Temat

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    Wyświetlanie 1-4 z 4
    Tytuł:
    The melting of native domain structure in effector activation of IgG studied by using Congo Red as a specific probe
    Autorzy:
    Piekarska, B
    Roterman, I.
    Rybarska, J.
    Konieczny, L.
    Kaszuba, J.
    Powiązania:
    https://bibliotekanauki.pl/articles/69497.pdf
    Data publikacji:
    1994
    Wydawca:
    Polskie Towarzystwo Fizjologiczne
    Tematy:
    immunoglobulin
    molten globule state
    Congo Red
    effector activity
    Źródło:
    Journal of Physiology and Pharmacology; 1994, 45, 1
    0867-5910
    Pojawia się w:
    Journal of Physiology and Pharmacology
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Denatured proteins and early folding intermediates simulated in a reduced conformational space
    Autorzy:
    Kmiecik, Sebastian
    Kurcinski, Mateusz
    Rutkowska, Aleksandra
    Gront, Dominik
    Kolinski, Andrzej
    Powiązania:
    https://bibliotekanauki.pl/articles/1041278.pdf
    Data publikacji:
    2006
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    sequence profiles
    statistical potentials
    protein folding intermediates
    high resolution lattice protein models
    Replica Exchange Monte Carlo
    molten globule
    protein folding
    Opis:
    Conformations of globular proteins in the denatured state were studied using a high-resolution lattice model of proteins and Monte Carlo dynamics. The model assumes a united-atom and high-coordination lattice representation of the polypeptide conformational space. The force field of the model mimics the short-range protein-like conformational stiffness, hydrophobic interactions of the side chains and the main-chain hydrogen bonds. Two types of approximations for the short-range interactions were compared: simple statistical potentials and knowledge-based protein-specific potentials derived from the sequence-structure compatibility of short fragments of protein chains. Model proteins in the denatured state are relatively compact, although the majority of the sampled conformations are globally different from the native fold. At the same time short protein fragments are mostly native-like. Thus, the denatured state of the model proteins has several features of the molten globule state observed experimentally. Statistical potentials induce native-like conformational propensities in the denatured state, especially for the fragments located in the core of folded proteins. Knowledge-based protein-specific potentials increase only slightly the level of similarity to the native conformations, in spite of their qualitatively higher specificity in the native structures. For a few cases, where fairly accurate experimental data exist, the simulation results are in semiquantitative agreement with the physical picture revealed by the experiments. This shows that the model studied in this work could be used efficiently in computational studies of protein dynamics in the denatured state, and consequently for studies of protein folding pathways, i.e. not only for the modeling of folded structures, as it was shown in previous studies. The results of the present studies also provide a new insight into the explanation of the Levinthal's paradox.
    Źródło:
    Acta Biochimica Polonica; 2006, 53, 1; 131-144
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Probing protein structure by limited proteolysis.
    Autorzy:
    Fontana, Angelo
    de Laureto, Patrizia Polverino
    Spolaore, Barbara
    Frare, Erica
    Picotti, Paola
    Zambonin, Marcello
    Powiązania:
    https://bibliotekanauki.pl/articles/1043265.pdf
    Data publikacji:
    2004
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    cytochrome c
    complementing fragments
    protein domains
    apomyoglobin
    lysozyme
    mass spectrometry
    α-lactalbumin
    limited proteolysis
    molten globule
    protein flexibility
    human growth hormone
    Opis:
    Limited proteolysis experiments can be successfully used to probe conformational features of proteins. In a number of studies it has been demonstrated that the sites of limited proteolysis along the polypeptide chain of a protein are characterized by enhanced backbone flexibility, implying that proteolytic probes can pinpoint the sites of local unfolding in a protein chain. Limited proteolysis was used to analyze the partly folded (molten globule) states of several proteins, such as apomyoglobin, α-lactalbumin, calcium-binding lysozymes, cytochrome c and human growth hormone. These proteins were induced to acquire the molten globule state under specific solvent conditions, such as low pH. In general, the protein conformational features deduced from limited proteolysis experiments nicely correlate with those deriving from other biophysical and spectroscopic techniques. Limited proteolysis is also most useful for isolating protein fragments that can fold autonomously and thus behave as protein domains. Moreover, the technique can be used to identify and prepare protein fragments that are able to associate into a native-like and often functional protein complex. Overall, our results underscore the utility of the limited proteolysis approach for unravelling molecular features of proteins and appear to prompt its systematic use as a simple first step in the elucidation of structure-dynamics-function relationships of a novel and rare protein, especially if available in minute amounts.
    Źródło:
    Acta Biochimica Polonica; 2004, 51, 2; 299-321
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Budowa i funkcje układów białkowo-lipidowych
    Structure and function of protein-lipid systems
    Autorzy:
    Litwińczuk-Mammadova, A.
    Cieślik-Boczula, K.
    Rospenk, M.
    Powiązania:
    https://bibliotekanauki.pl/articles/972303.pdf
    Data publikacji:
    2016
    Wydawca:
    Polskie Towarzystwo Chemiczne
    Tematy:
    odziaływania białko-lipid
    liposomy DPPC
    przejścia fazowe
    α-laktoalbumina
    kompleks HAMLET/BAMLET
    stopiona globula
    lipid-protein interactions
    DPPC liposomes
    phase transitions
    α-lactalbumin
    complex HAMLET/BAMLET
    molten globule state
    Opis:
    Biomembranes play many structural and functional roles in both prokaryotic and eukaryotic cells [10]. They define compartments, the communication between the inside and outside of the cell. The main components of biomembranes are lipids and proteins, which form protein-lipid bilayer systems [10]. A structure and physicochemical properties of protein-lipid membranes, which determines biological activities of biomembranes, are strongly dependent on interactions between lipid and protein components and external agents such as a temperature, pH, and a membrane hydration [4]. A lipid bilayer matrix serves as a perfect environment for membrane proteins (Fig. 1), and it assures activities of these proteins. Because biomembranes are composed of many different groups of lipids and proteins and have a complex structure, it is difficult to study in details their physicochemical properties using physicochemical methods. For these reason, lipid membranes of liposomes are used in many scientific laboratories for studding processes associated with a lipid phase transition, a membrane hydration, or protein-membrane interactions. The structure of liposomes (Fig. 5), and an influence of pH and an ionic strength on a lipid bilayer structure are discussed in the presented work. The role of membrane proteins in determination of biological activities of biomembranes is highlighted. A high variety of a structure and an enzymatic activity of membrane proteins is responsible for a high diversity of biological functions of cell membranes [2]. α-Lactalbumin (α-LA) is a peripheral membrane protein (Figs 8 and 9), its biological function is strongly related to its conformational structure and interaction with lipid membranes [49]. The complex of α-LA in a molten globule conformational state with oleic acid, termed as a HAMLET complex, are disused in a context of its anti-tumor activity.
    Źródło:
    Wiadomości Chemiczne; 2016, 70, 11-12; 723-746
    0043-5104
    2300-0295
    Pojawia się w:
    Wiadomości Chemiczne
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-4 z 4

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