↓ Direkt till sidans innehåll
↓ Direkt till sidans sekundära innehåll (sidomenyn)

Träfflista för sökning "WFRF:(Tapia I) srt2:(1995-1999)"

Search: WFRF:(Tapia I) > (1995-1999)

Result 1-9 of 9

Sort/group result

Sort by: Hits per page:

Enumeration	Reference	Cover	Find
1.	Dunham, I, et al. (author) The DNA sequence of human chromosome 22 1999 In: Nature. - : Springer Science and Business Media LLC. - 0028-0836 .- 1476-4687. ; 402:6761, s. 489-495 Journal article (peer-reviewed)
2.	Arteca, GA, et al. (author) Unfolded in vacuo lysozyme folds into native, quasinative, and compact structures 1999 In: PHYSICAL REVIEW E. - : AMERICAN PHYSICAL SOC. - 1063-651X. ; 59:5, s. 5981-5986 Journal article (peer-reviewed)abstract We show that the relaxation dynamics of unfolded in vacuo lysozyme is not random. Analyses of molecular dynamics trajectories in a convenient space of molecular shape descriptors reveal a "favored" pattern of transitions leading to stable conformations. T
3.	Arteca, GA, et al. (author) Variations in chain compactness and topological complexity uncover folding processes in the relaxation dynamics of unfolded in vacuo lysozyme 1999 In: JOURNAL OF CHEMICAL PHYSICS. - : AMER INST PHYSICS. - 0021-9606. ; 111:10, s. 4774-4779 Journal article (other academic/artistic)abstract Chain collapse and the formation of a near-native tertiary structure are believed to be two key features controlling the progress of a protein folding transition. In this work, we study the interrelation between these two properties along computer-simulat
4.	Reimann, CT, et al. (author) Conformation of highly-charged gas-phase lysozyme revealed by energetic surface imprinting 1998 In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - : AMER CHEMICAL SOC. - 0002-7863. ; 120:30, s. 7608-7616 Journal article (other academic/artistic)abstract We present new results from an energetic surface imprinting method which allows us to outline the general conformation of protein ions in vacuo. Both disulfide-bond-intact and disulfide-bond-reduced gasphase lysozyme ions were produced by electrospray ion
5.	Reimann, CT, et al. (author) Proteins in vacuo: A molecular dynamics study of the unfolding behavior of highly charged disulfide-bond-intact lysozyme subjected to a temperature pulse 1999 In: PHYSICAL REVIEW E. - : AMERICAN PHYSICAL SOC. - 1063-651X. ; 60:6, s. 7277-7284 Journal article (peer-reviewed)abstract Molecular dynamics simulations were used to interpret a variety of experimental data on highly charged disulfide-bond-intact lysozyme in vacuo. The simulation approach involved submitting a model of the protein [Reimann, Velazquez, and Tapia, J. Phys. Che
6.	Reimann, CT, et al. (author) Proteins in vacuo. Denaturation of highly-charged lysozyme studied by molecular dynamics simulations 1998 In: JOURNAL OF PHYSICAL CHEMISTRY B. - : AMER CHEMICAL SOC. - 1089-5647. ; 102:46, s. 9344-9352 Journal article (other academic/artistic)abstract Molecular dynamics (MD) simulations have been employed to address the structural changes of lysozyme (LYZ) in vacuo driven by Coulomb forces associated with multiple protonation, as occurs in electrospray ionization. Some general features which emerged fr
7.	Reimann, CT, et al. (author) Proteins in vacuo. Denaturing of disulfide-intact and disulfide-broken lysozyme probed by molecular dynamics simulations 1998 In: JOURNAL OF PHYSICAL CHEMISTRY B. - : AMER CHEMICAL SOC. - 1089-5647. ; 102:12, s. 2277-2283 Journal article (other academic/artistic)abstract Proteins in vacuo are the subject of a number of experimental techniques where unfolding has been shown to be an important feature. In this paper we report on a detailed structural study of protein denaturation modeled in molecular dynamics (MD) simulatio
8.	Tapia, O, et al. (author) Molecular dynamics simulations of DNA with protein's consistent GROMOS force field and the role of counterions' symmetry 1997 In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - : AMER CHEMICAL SOC. - 0002-7863. ; 119:25, s. 5934-5938 Journal article (peer-reviewed)abstract Model solvent effects, related to DNA stability in water, are explored with molecular dynamics (MD) simulations: (i) hydrophobicity and (ii) salt modulated electrostatic effects. The 2.6 Angstrom resolution X-ray coordinates of the DNA oligomer from Zif26
9.	Velazquez, I, et al. (author) Proteins in vacuo: Relaxation of unfolded lysozyme leads to folding into native and non-native structures. A molecular dynamics study 1999 In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - : AMER CHEMICAL SOC. - 0002-7863. ; 121:49, s. 11468-11477 Language: English Journal article (peer-reviewed)abstract Unfolding and refolding processes for proteins in vacuo and gas phase are becoming the subject of experimental and theoretical attention. Recently, a molecular dynamics study of unfolding of disulfide-bond-intact lysozyme (DI-LYZ) in vacuo showed large-sc

Skapa referenser, mejla, bekava och länka

Permalink

Result 1-9 of 9

Refine your search

Type of publication: journal article (9)

Type of content: peer-reviewed (5); other academic/artistic (4)

Author/Editor: Tapia, O (8); Velazquez, I (8); Reimann, CT (7); Arteca, GA (2); Beck, S (1); Chen, Y. (1); show more...; Williams, S. (1); Sasaki, T. (1); Zhang, G (1); Wang, Y. (1); Nguyen, T. (1); Hall, C (1); Du, Z. (1); Nelson, J. (1); Williams, L. (1); Wang, Z. (1); Lewis, J (1); Miller, N (1); Shibuya, K (1); Shimizu, N. (1); Scheet, P (1); Wang, Q. (1); Yao, Z. (1); Dunham, I (1); Chen, F (1); Hall, R (1); Ren, Q (1); Matthews, L (1); King, A (1); Axelsson, J (1); Johnson, D. (1); Pearson, D. (1); Fang, F (1); Chu, L (1); Wu, H. (1); Fulton, R (1); Wilson, R (1); Pan, H. (1); Hunt, SE (1); Song, L. (1); Hawkins, J. (1); Murray, J. (1); Johnson, A (1); Buck, D (1); Dumanski, JP (1); Conroy, D. (1); Aoki, N. (1); Qian, Y (1); Davis, J. (1); Do, T (1); show less...

University: Uppsala University (8); Karolinska Institutet (1)

Language: English (9)

Year

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

Copyright © LIBRIS - National Library Systems
LIBRIS.kb.se

pil uppåt

Close

Copy and save the link in order to return to this view