Results 91 to 100 of about 3,579,241 (217)

SCREENING INTERACTIONS BETWEEN PROTEINS AND DISORDERED PEPTIDES BY A NOVEL COMPUTATIONAL METHOD [PDF]

open access: yes, 2013
Concerted interactions between proteins in cells form the basis of most biological processes. Biophysicists study protein–protein association by measuring thermodynamic and kinetic properties.
Zhang, Weiyi
core  

Buried and accessible surface area control intrinsic protein flexibility [PDF]

open access: yes, 2013
Proteins experience a wide variety of conformational dynamics that can be crucial for facilitating their diverse functions. How is the intrinsic flexibility required for these motions encoded in their three-dimensional structures?
Marsh, Joseph A; id_orcid
core   +1 more source

Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]

open access: yes, 2014
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Hardwick, Kevin G.   +20 more
core   +1 more source

Rethinking Gene Regulatory Networks in Light of Alternative Splicing, Post-Translational Modifications, and Intrinsically Disordered Protein Domains

open access: yesFrontiers in Cell and Developmental Biology, 2015
Models for genetic regulation and cell fate specification characteristically assume that gene regulatory networks (GRNs) are essentially deterministic and exhibit multiple stable states specifying alternate, but pre-figured cell fates. Mounting evidence
Karl J. Niklas   +3 more
doaj   +1 more source

Polymer Concepts in Cellular Function

open access: yes
Advanced Science, EarlyView.
Miao Yu   +7 more
wiley   +1 more source

Building coiled coils with polar cores

open access: yesProtein Science, Volume 35, Issue 10, October 2026.
Abstract Coiled coils are formed by α‐helices winding around each other into superhelical bundles. They are characterized by a specific geometry of interaction, called knobs‐into‐holes, in which residues in the core of the structure mesh regularly along a seam that runs the length of the helices.
Marcus D. Hartmann   +3 more
wiley   +1 more source

The function of intrinsically disordered selenoproteins

open access: yes, 2023
Rozovsky, SharonSELENOS and SELENOK are intrinsically disordered selenoproteins that take part in the endoplasmic-reticulum-associated degradation (ERAD) pathway, which degrades misfolded proteins and maintains cellular protein hemostasis.
Cheng, Rujin
core   +1 more source

AlphaFold2 modeling and molecular dynamics simulations of an intrinsically disordered protein.

open access: yesPLoS ONE
We use AlphaFold2 (AF2) to model the monomer and dimer structures of an intrinsically disordered protein (IDP), Nvjp-1, assisted by molecular dynamics (MD) simulations.
Hao-Bo Guo   +7 more
doaj   +1 more source

Impact of Stabilizing Osmolytes on the Conformational Dynamics of Human and Rat Islet Amyloid Polypeptides

open access: yesProteins: Structure, Function, and Bioinformatics, Volume 94, Issue 10, Page 1717-1737, October 2026.
ABSTRACT The aggregation of human islet amyloid polypeptide (hIAPP) into cytotoxic oligomers and amyloid fibrils is a hallmark of type 2 diabetes mellitus (T2DM), leading to pancreatic β‐cell dysfunction. In contrast, rat IAPP (rIAPP) is largely non‐amyloidogenic. Osmolytes such as glucose, glycerol, and sorbitol are known to stabilize globular protein
Kiara A. Kidman   +3 more
wiley   +1 more source

Nucleic Acids as Emerging Regulators of Calcium Phosphate Biomineralization

open access: yesThe FASEB Journal, Volume 40, Issue 17, 15 September 2026.
Calcium phosphate biomineralization has traditionally been considered a protein‐regulated process. This review highlights the emerging role of nucleic acids, which interact with mineral phases through adsorption, coprecipitation, and templating, thereby influencing crystal nucleation and growth.
Fanny Duhalde   +2 more
wiley   +1 more source

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