Zobrazeno 1 - 10 of 23 pro vyhledávání: '"Jean Ramstein"'
1
Stability and physicochemical properties of the bovine brain phosphatidylethanolamine-binding protein
Autor: Françoise Schoentgen, Nicole Bureaud, Caroline Teyssier, Régine Maget-Dana, Béatrice Vallée, Jean Ramstein
Publikováno v: European Journal of Biochemistry
European Journal of Biochemistry, Wiley, 1999, 266 (1), pp.40-52
International audience; The equilibrium behaviour of the bovine phosphatidylethanolamine-binding protein (PEBP) has been studied under various conditions of pH, temperature and urea concentration. Far-UV and near-UV CD, fluorescence and Fourier trans
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5630fb2f5d2da6be917df73ef57e6e1a
https://doi.org/10.1046/j.1432-1327.1999.00812.x
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2
Solvent-induced Structural Distortions of Horse Metmyoglobin
Autor: P. Calmettes, Bernard Alpert, Peter Martel, Jean Ramstein, Jean-Marie Glandières, A. Massat, Christian Zentz
Publikováno v: European Journal of Biochemistry. 227:241-248
Structural and dynamic constraints produced by the surrounding solvent on the aquometmyoglobin molecule were investigated by means of circular dichroism and Fourier-transform infrared spectroscopies, tritium/hydrogen exchange kinetics and small-angle
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::233302302c43277316abba1447c7ff52
https://doi.org/10.1111/j.1432-1033.1995.tb20381.x
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4
Base pairing at the stem-loop junction in the SL1 kissing complex of HIV-1 RNA: a thermodynamic study probed by molecular dynamics simulation
Autor: Jean Ramstein, Samia Aci, Daniel Genest
Publikováno v: Journal of Biomolecular Structure and Dynamics
Journal of Biomolecular Structure and Dynamics, Taylor & Francis: STM, Behavioural Science and Public Health Titles, 2004, 21, pp.833-839
The thermodynamics of the opening/closure process of a GC base pair located at the stem-loop junction of the SL1 sequence from HIV-1(Lai) genomic RNA was investigated in the context of a loop-loop homodimer (or kissing complex) using molecular dynami
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bbc472433c5b299fa2390bf610ae196
https://pubmed.ncbi.nlm.nih.gov/15107005
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5
Evidence of a thermal unfolding dimeric intermediate for the Escherichia coli histone-like HU proteins: thermodynamics and structure
Autor: Charles Zelwer, Franck Coste, Bertrand Castaing, Jean Ramstein, Jacques Oberto, Nadège Hervouet
Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2003, 331 (1), pp.101-21
HAL
International audience; The Escherichia coli histone-like HU protein pool is composed of three dimeric forms: two homodimers, EcHUalpha(2) and EcHUbeta(2), and a heterodimer, EcHUalphabeta. The relative abundance of these dimeric forms varies during
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f78887688a41aa17ee69e4d5a594f833
https://hal.archives-ouvertes.fr/hal-02127656
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6
Domain-domain interactions in high mobility group 1 protein (HMG1)
Autor: Marco Bianchi, Daniel Locker, Jean Ramstein, Marc Leng
Publikováno v: European journal of biochemistry. 260(3)
The high mobility group protein HMG1 is a conserved chromosomal protein with two homologous DNA-binding domains, A and B, and an acidic carboxy-terminal tail, C. The structure of isolated domains A and B has been previously determined by NMR, but the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4cd6552ce664cffc5e11a031e082424
https://pubmed.ncbi.nlm.nih.gov/10102997
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7
Solvent effects on horse apomyoglobin dynamics
Autor: Patrick Tauc, Jean Ramstein, Bernard Alpert, Ahmed Haouz, Serge Pin, Jean-Marie Glandières, Jean-Claude Brochon, Christian Zentz
Publikováno v: Biochemistry. 37(9)
The effects of the solvent conditions (buffer pH 9, 8, or 7 or buffer pH 6.5 alone or mixed with 3.2% ethanol or 6.2% formamide) on the protein dynamics of horse apomyoglobin were investigated through tryptophan fluorescence quenching, spectra, and d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6198df7c93893211cdcfd41a904f9dc6
https://pubmed.ncbi.nlm.nih.gov/9485453
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8
Rotational Motions of Bases in DNA
Autor: Jean Ramstein, F. Briki, Daniel Genest, Richard Lavery
Publikováno v: Modelling of Biomolecular Structures and Mechanisms ISBN: 9789401042222
Two different kinds of dynamics simulation have been performed to investigate the rotation of the bases in DNA. A Brownian dynamics simulation using data from fluorescence experiments establishes a link between the rotation observed at the nanosecond
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ce9d453a3ac68015a7089ba4f554b7d5
https://doi.org/10.1007/978-94-011-0497-5_19
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9
A reexamination of the stopped-flow measured hydrogen-deuterium exchange rates in nucleic acid double helices
Autor: Jean-Luc Girardet, Jean Ramstein
Publikováno v: Biochimica et biophysica acta. 1130(2)
Using the deuteration labelling method in conjunction with an improved stopped-flow instrument, we have reexamined the proton exchange process in poly(dA-dT).poly(dA-dT). A single proton exchange class is found with a rate constant at 20 degrees C of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e19efa00dd0dd3c4291d1096b041625
https://pubmed.ncbi.nlm.nih.gov/1314090
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10
Base pair opening pathways in B-DNA
Autor: Jean Ramstein, Richard Lavery
Publikováno v: Journal of Biomolecular Structure and Dynamics
Journal of Biomolecular Structure and Dynamics, Taylor & Francis: STM, Behavioural Science and Public Health Titles, 1990, 7, pp.915-933
ResearcherID
International audience; Molecular modeling is used to study the opening pathways of bases within a B-DNA oligomer. It is demonstrated that many open states are possible for a single base pair, although a preference for opening towards the major groov
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d04d4d88ce84a22ed5bc3ac3ac55e39
https://hal.archives-ouvertes.fr/hal-00313447
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