Tilt angle conformational landscapes of residues involved in 1-to-1 helix contacts during the last 500 ns of trajectory in the Surface model.

Results for helices 1, 2 and 3 shown in the left, middle and right columns, and replicas 1, 2, 3 and 4 shown in the corresponding rows. Yellow rectangles indicate populated regions conserved across all Bound replicas. (TIFF)

Guardado en:

Detalles Bibliográficos
Autor principal:	Oluwatoyin Campbell (14392137) (author)
Otros Autores:	Dina Dahhan (22683620) (author), Viviana Monje (2056069) (author)
Publicado:	2025
Materias:	Biophysics Biochemistry Cell Biology Genetics Molecular Biology Biotechnology Cancer Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Physical Sciences not elsewhere classified Information Systems not elsewhere classified process may help complex transmembrane topology comparing dimer interactions aqueous solution versus promote p7 oligomerization protein residue alignment p7 dimers driven alignment underlie health study demonstrates particularly involving often composed molecular mechanisms key residues hydrophobic contacts hydrogen bonding first helix explain assembly dynamic contributors channel assembly
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

Sea el primero en dejar un comentario!

Tilt angle conformational landscapes of residues involved in 1-to-1 helix contacts during the last 500 ns of trajectory in the <i>Surface</i> model.

Ejemplares similares