Results 1 to 10 of about 707,163 (239)

Protein conformation and biomolecular condensates [PDF]

open access: yesCurrent Research in Structural Biology, 2022
Protein conformation and cell compartmentalization are fundamental concepts and subjects of vast scientific endeavors. In the last two decades, we have witnessed exciting advances that unveiled the conjunction of these concepts. An avalanche of studies highlighted the central role of biomolecular condensates in membraneless subcellular ...
Mario R Ermacora
exaly   +5 more sources

Conformations of Proteins in Equilibrium [PDF]

open access: yesPhysical Review Letters, 2001
6 pages, 3 eps ...
Micheletti, Cristian   +2 more
openaire   +4 more sources

Mechano-transduction: from molecules to tissues. [PDF]

open access: yes, 2014
External forces play complex roles in cell organization, fate, and homeostasis. Changes in these forces, or how cells respond to them, can result in abnormal embryonic development and diseases in adults.
Dunn, Alexander R   +3 more
core   +2 more sources

Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor [PDF]

open access: yes, 2010
We report the 'early' conformation of the Escherichia coli signal recognition particle (SRP) and its receptor FtsY bound to the translating ribosome, as determined by cryo-EM.
Ban, Nenad   +4 more
core   +1 more source

Structural interrogation of phosphoproteome identified by mass spectrometry reveals allowed and disallowed regions of phosphoconformation [PDF]

open access: yes, 2014
High-throughput mass spectrometric (HT-MS) study is the method of choice for monitoring global changes in proteome. Data derived from these studies are meant for further validation and experimentation to discover novel biological insights.
Balakrishnan, Satish   +4 more
core   +2 more sources

Limited proteolysis in the investigation of beta2-microglobulin amyloidogenic and fibrillar states. [PDF]

open access: yes, 2005
Amyloid fibrils of patients treated with regular haemodialysis essentially consists of β2-microglobulin (β2-m) and its truncated species ΔN6β2-m lacking six residues at the amino terminus.
AMORESANO, ANGELA   +4 more
core   +1 more source

Pyrene: A Probe to Study Protein Conformation and Conformational Changes [PDF]

open access: yesMolecules, 2011
The review focuses on the unique spectral features of pyrene that can be utilized to investigate protein structure and conformation. Pyrene is a fluorescent probe that can be attached covalently to protein side chains, such as sulfhydryl groups. The spectral features of pyrene are exquisitely sensitive to the microenvironment of the probe: it exhibits ...
Arti B. Patel   +2 more
openaire   +3 more sources

Conformational kinetics reveals affinities of protein conformational states [PDF]

open access: yesProceedings of the National Academy of Sciences, 2015
Significance Despite 50 years of studies of coupled binding and conformational change reactions in proteins and nucleic acids, there has been no detailed analysis of the affinities of the multiple conformational states involved. The relationship between these affinities and the dynamics of conformational change has also been largely ...
Daniels, Kyle G   +2 more
openaire   +2 more sources

Tracing conformational changes in proteins [PDF]

open access: yes2009 IEEE International Conference on Bioinformatics and Biomedicine Workshop, 2009
Many proteins undergo extensive conformational changes as part of their functionality. Tracing these changes is important for understanding the way these proteins function. Traditional biophysics-based conformational search methods require a large number of calculations and are hard to apply to large-scale conformational motions.In this work we ...
Haspel, Nurit   +4 more
openaire   +3 more sources

Identifying the protein folding nucleus using molecular dynamics [PDF]

open access: yes, 2000
Molecular dynamics simulations of folding in an off-lattice protein model reveal a nucleation scenario, in which a few well-defined contacts are formed with high probability in the transition state ensemble of conformations.
Buldyrev, Sergey V.   +3 more
core   +1 more source

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