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Wyszukujesz frazę "protein tertiary structure" wg kryterium: Temat


Wyświetlanie 1-3 z 3
Tytuł:
Structure of small G proteins and their regulators.
Autorzy:
Paduch, Marcin
Jeleń, Filip
Otlewski, Jacek
Tematy:
small G protein
GAP
protein-protein interaction
GTPase
GDI
Rho
Ras
protein tertiary structure
GEF
Pokaż więcej
Wydawca:
Polskie Towarzystwo Biochemiczne
Powiązania:
https://bibliotekanauki.pl/articles/1043851.pdf  Link otwiera się w nowym oknie
Opis:
In recent years small G proteins have become an intensively studied group of regulatory GTP hydrolases involved in cell signaling. More than 100 small G proteins have been identified in eucaryotes from protozoan to human. The small G protein superfamily includes Ras, Rho Rab, Rac, Sar1/Arf and Ran homologs, which take part in numerous and diverse cellular processes, such as gene expression, cytoskeleton reorganization, microtubule organization, and vesicular and nuclear transport. These proteins share a common structural core, described as the G domain, and significant sequence similarity. In this paper we review the available data on G domain structure, together with a detailed analysis of the mechanism of action. We also present small G protein regulators: GTPase activating proteins that bind to a catalytic G domain and increase its low intrinsic hydrolase activity, GTPase dissociation inhibitors that stabilize the GDP-bound, inactive state of G proteins, and guanine nucleotide exchange factors that accelerate nucleotide exchange in response to cellular signals. Additionally, in this paper we describe some aspects of small G protein interactions with downstream effectors.
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Role of disulfide bonds in stabilizing the conformation of selected enzymes : an approach based on divergence entropy applied to the structure of hydrophobic core in proteins
Autorzy:
Kalinowska, Barbara
Banach, Mateusz
Roterman-Konieczna, Irena
Konieczny, Leszek
Opis:
One of the factors responsible for tertiary structural stabilization in proteins is the presence of the hydrophobic core—a result of hydrophobic interactions within the protein body. In some proteins (especially extracellular ones) additional stabilization is provided by covalent bonds between selected Cys residues, commonly referred to as disulfide bonds. The mutual interplay of both factors and their respective contributions to stabilization are the focus of this work. The assessment of the effects of disulfide bonds isinterpreted by Fuzzy Oil Drop (FOD) model in which individual polypeptide chain fragments (including fragments which participate in SS bonds) can be evaluated in the context of their influence upon tertiary structural stabilization by comparing their corresponding theoretical and idealized hydrophobicity density distributions. The proteins were identified with both factors reinforcing each other, as well as proteins where they seem to counteract each other. The analysis presents a number of enzymes, including ribonuclease, lysozyme, disulfide isomerase and phospholipase.
Dostawca treści:
Repozytorium Uniwersytetu Jagiellońskiego
Artykuł
Tytuł:
Correlated mutations in selected protein families
Autorzy:
Leluk, J.
Sobczyk, M.
Becella, Ł.
Tematy:
protein sequence
multiple alignment
tertiary structure
mutational correlation
genetic semihomology algorithm
Pokaż więcej
Wydawca:
Politechnika Gdańska
Powiązania:
https://bibliotekanauki.pl/articles/1986920.pdf  Link otwiera się w nowym oknie
Opis:
Four different protein families (two proteinase inhibitor families, myoglobins and lysozymes) were surveyed for correlated mutations with respect to the position distance and their significance in structure stabilization and biological activity. They were chosen for this study in order to verify the currently admitted model of mutational correlation relationship with respect to spatial contact of the residues and contribution in protein biological activity. There was observed high contribution of spatially dispersed residues (which are also not involved in the protein active center) in mutational correlation. Because of the significantly large distance between correlated positions these cases do not correspond explicitly to any mechanism included in current hypotheses. It is suggested that the role of residue spatial contact in structure preservation, intermolecular interaction and active site rescue mechanisms only partially explains the correlation phenomenon.
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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