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Science

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Disponibilidad
Institución detectada Período Navegá Descargá Solicitá
No detectada desde mar. 1997 / hasta dic. 2023 Science Journals

Información

Tipo de recurso:

revistas

ISSN impreso

0036-8075

ISSN electrónico

1095-9203

Editor responsable

American Association for the Advancement of Science (AAAS)

País de edición

Estados Unidos

Fecha de publicación

Cobertura temática

Tabla de contenidos

Editors' Choice

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1580-1581

Dogs return to the show

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1580.1-1580

A bacterial battleground

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1580.2-1581

Identifying the weakest links

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1580.3-1581

Carotenoids drive chromoplast development

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1580.4-1581

Identity by association

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1580.5-1581

Merging across the black hole mass gap

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1580.6-1581

Cyclopropanes through C–H activation

Caroline Ash; Jesse Smith (eds.)

Palabras clave: Multidisciplinary.

Pp. 1580.7-1581

Distinct conformational states of SARS-CoV-2 spike protein

Yongfei CaiORCID; Jun Zhang; Tianshu XiaoORCID; Hanqin PengORCID; Sarah M. SterlingORCID; Richard M. WalshORCID; Shaun RawsonORCID; Sophia Rits-Volloch; Bing ChenORCID

<jats:title>A dynamic viral spike</jats:title> <jats:p> Efforts to protect human cells against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have focused on the trimeric spike (S) protein. Several structures have shown a stabilized ectodomain of the spike in its prefusion conformation. Cai <jats:italic>et al.</jats:italic> now provide insight into the structural changes in the S protein that result in the fusion of the viral and host cell membranes. They purified full-length S protein and determined cryo–electron microscopy structures of both the prefusion and postfusion conformations. These structures add to our understanding of S protein function and could inform vaccine design. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6511" page="1586" related-article-type="in-this-issue" vol="369" xlink:href="10.1126/science.abd4251">1586</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 1586-1592

Rotational resonances in the H 2 CO roaming reaction are revealed by detailed correlations

Mitchell S. QuinnORCID; Klaas Nauta; Meredith J. T. Jordan; Joel M. BowmanORCID; Paul L. HoustonORCID; Scott H. KableORCID

<jats:title> Duality of roaming mechanism in H <jats:sub>2</jats:sub> CO </jats:title> <jats:p> The phenomenon of roaming in chemical reactions (that is, bypassing the minimum energy pathway from unlikely geometries) has attracted a great deal of attention in the chemical reaction dynamics community over the past decade and still demonstrates unexpected results. Using velocity-map imaging of state-selected H <jats:sub>2</jats:sub> products of H <jats:sub>2</jats:sub> CO photodissociation, Quinn <jats:italic>et al.</jats:italic> discovered the bimodal structure of rotational distribution of the other product fragment, CO. Quasiclassical trajectories showed that this bimodality originates from two distinctive reaction pathways that proceed by the trans or cis configuration of O–C–H⋯H, leading to high or low rotational excitations of CO, respectively. Whether such a mechanism is present in the many other chemical reactions for which roaming reaction pathways have been reported is yet to be determined. </jats:p> <jats:p> <jats:italic>Science</jats:italic> , this issue p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="6511" page="1592" related-article-type="in-this-issue" vol="369" xlink:href="10.1126/science.abc4088">1592</jats:related-article> </jats:p>

Palabras clave: Multidisciplinary.

Pp. 1592-1596