Home
About
Overview
Sharing Data
ORCID
Help
History (24)
Functional analysis of Tpr: identification of nuclear pore complex association and nuclear localization domains and a role in mRNA export.
The crystal structure of the GroES co-chaperonin at 2.8 A resolution.
Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.
Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones.
Roles of beta-turns in protein folding: from peptide models to protein engineering.
See All 24 Pages
Login
to edit your profile (add a photo, awards, links to other websites, etc.)
Edit My Profile
My Person List (
0
)
Return to Top
Roles of beta-turns in protein folding: from peptide models to protein engineering.
Marcelino AM, Gierasch LM. Roles of beta-turns in protein folding: from peptide models to protein engineering. Biopolymers. 2008 May; 89(5):380-91.
View in:
PubMed
subject areas
Models, Molecular
Peptides
Protein Engineering
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
authors with profiles
Lila M Gierasch Ph.D.