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Non-functional conserved residues in globins and their possible role as a folding nucleus 1 1Edited by F. E. Cohen

Autor: Ptitsyn Ob, Kai-Li H Ting

Publikováno v: Journal of Molecular Biology. 291:671-682

Structure-based sequence alignment of 728 sequences of different globin subfamilies shows that in each subfamily there are two clusters of consensually conserved residues. The first is the well-known “functional” cluster which includes six heme-b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1a59d25dd724a07d95dd41d013004b07
https://doi.org/10.1006/jmbi.1999.2920

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All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins

Autor: Vladimir N. Uversky, Ptitsyn Ob

Publikováno v: Folding and Design. 1:117-122

Backgound: It has long been established that temperature-induced melting of small globular proteins is an all-or-none transition. Little was known, however, about the degree of cooperativity of denaturant-induced transitions in proteins, especially i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35b89497588a06ba98ceb2936d5035fb
https://doi.org/10.1016/s1359-0278(96)00020-x

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Molten Globule-Like State of Cytochrome c under Conditions Simulating Those Near the Membrane Surface

Autor: Elisaveta I. Tiktopulo, Vladimir N. Uversky, Stanislav I. Klenin, Alexandra E. Dujsekina, V. E. Bychkova, Ptitsyn Ob

Publikováno v: Biochemistry. 35:6058-6063

Methanol-induced conformational transitions in cytochrome c have been studied by near- and far-UV circular dichroism, Trp fluorescence, microcalorimetry, and diffusion measurements. The existence of at least two cooperative stages of transition has b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65168641059e5d61f7fba6e718eaf867
https://doi.org/10.1021/bi9522460

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A new approach to artificial and modified proteins: theory-based design, synthesis in a cell-free system and fast testing of structural properties by radiolabels

Autor: V.V. Chemeris, Ptitsyn Ob, Kirpichnikov Mp, Alexey V. Finkelstein, Dmitry A. Dolgikh, A. N. Fedorov, Vladimir N. Uversky

Publikováno v: "Protein Engineering, Design and Selection". 7:1041-1052

A novel approach to the creation of artificial and modified proteins has been elaborated. The approach includes a sequence design based on the molecular theory of protein secondary structure and folding patterns, gene expression in a cell-free system

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::212312fb34cd00d752605850a5fb9e7e
https://doi.org/10.1093/protein/7.8.1041

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Molten globule versus variety of intermediates: influence of anions on pH-denatured apomyoglobin

Autor: Olga Tcherkasskaya, Ptitsyn Ob

Publikováno v: FEBS letters. 455(3)

The molten globule state was shown to be the third thermodynamic state of protein molecules in addition to their native and unfolded states. On the other hand, it was reported that optical and hydrodynamic properties of pH-denatured apomyoglobin depe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51e35b21210747837ce684f74d9c3d1d
https://pubmed.ncbi.nlm.nih.gov/10437798

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Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes?

Autor: Ptitsyn Ob

Publikováno v: Journal of molecular biology. 278(3)

Amino acid sequences of seven subfamilies of cytochromes c (mitochondrial cytochromes c, c1; chloroplast cytochromes c6, cf; bacterial cytochromes c2, c550, c551; in total 164 sequences) have been compared. Despite extensive homology within eukaryoti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e66ca3494289dff6e17431aa2840d8b2
https://pubmed.ncbi.nlm.nih.gov/9600846

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Empirical Solvent-Mediated Potentials Hold For Both Intra-Molecular And Inter-Molecular Inter-Residue Interactions

Autor: Keskin, O, Bahar, I, Badretdinov, AY, Ptitsyn, OB, Jernigan, RL

Whether knowledge-based intra-molecular inter-residue potentials are valid to represent inter-molecular interactions taking place at protein-protein interfaces has been questioned in several studies. Differences in the chain connectivity effect and i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=r39c86a4b39b::0adcf9c1040099b0f9b1fec23c918397
https://aperta.ulakbim.gov.tr/record/101591

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Further evidence on the equilibrium 'pre-molten globule state': four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature

Autor: Vladimir N. Uversky, Ptitsyn Ob

Publikováno v: Journal of molecular biology. 255(1)

Equilibrium guanidinium chloride-induced unfolding of bovine carbonic anhydrase NB has been investigated by a combination of optical methods with size-exclusion chromatography. It has been shown that, as in the case of staphylococcal beta-lactamase,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7e89edc53f133514ddb69da1b711fae
https://pubmed.ncbi.nlm.nih.gov/8568868

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Folding intermediates are involved in genetic diseases?

Autor: Ptitsyn Ob, V. E. Bychkova

Publikováno v: FEBS letters. 359(1)

Recent experimental data show that some human genetic diseases are due to mutations in proteins which influence their trafficking and lead to retaining of proteins in the endoplasmic reticulum or their unproper processing. In this paper a hypothesis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5d71193bacad418c5756852a152ac30
https://pubmed.ncbi.nlm.nih.gov/7531653

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