Results 81 to 90 of about 3,841,423 (288)
Elucidating ATP’s role as solubilizer of biomolecular aggregate
Proteins occurring in significantly high concentrations in cellular environments (over 100 mg/ml) and functioning in crowded cytoplasm, often face the prodigious challenges of aggregation which are the pathological hallmark of aging and are critically ...
Susmita Sarkar +4 more
doaj +1 more source
Development of Charge-Augmented Three-Point Water Model (CAIPi3P) for Accurate Simulations of Intrinsically Disordered Proteins [PDF]
Intrinsically disordered proteins (IDPs) are molecules without a fixed tertiary structure, exerting crucial roles in cellular signalling, growth and molecular recognition events. Due to their high plasticity, IDPs are very challenging in experimental and
Agnieszka K., Bronowska +2 more
core +1 more source
Vacuolar H+‐ATPase (V‐ATPase) is a multisubunit rotary proton pump that acidifies intracellular compartments. Using elastic network models, we identified conserved hinge residues that govern its large‐scale functional motions. We show that intrinsically encoded ‘soft modes’ drive critical functional transitions, including rotary catalysis and ...
Diksha Parwana +3 more
wiley +1 more source
Ensemble Docking for Intrinsically Disordered Proteins
Abstract Intrinsically disordered proteins (IDPs) are implicated in many human diseases and are increasingly being pursued as drug targets. Conventional structure-based drug design methods that rely on well-defined binding sites are however, largely unsuitable for IDPs.
Anjali Dhar +2 more
openaire +3 more sources
Many studies about classification and the functional annotation of intrinsically disordered proteins (IDPs) are based on either the occurrence of long disordered regions or the fraction of disordered residues in the sequence.
Antonio Deiana +3 more
doaj +1 more source
With the exponential increase in the number of sequenced organisms, automated annotation of proteins is becoming increasingly important. Intrinsically disordered regions are known to play a significant role in protein function.
Alok Sharma +6 more
doaj +1 more source
New insights into disordered proteins and regions according to the FOD-M model.
A collection of intrinsically disordered proteins (IDPs) having regions with the status of intrinsically disordered (IDR) according to the Disprot database was analyzed from the point of view of the structure of hydrophobic core in the structural unit ...
Irena Roterman +3 more
doaj +1 more source
SCREENING INTERACTIONS BETWEEN PROTEINS AND DISORDERED PEPTIDES BY A NOVEL COMPUTATIONAL METHOD [PDF]
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
Mechanisms of change in protein architecture [PDF]
Proteins are the basic building blocks and functional units in all living organisms. Moreover, differences between species can frequently be explained with differences in their protein complements.
core +2 more sources
Unlocking the potential of cell‐permeable nanobodies for intracellular applications
This review outlines current strategies for delivery of nanobodies into cells and highlights recent examples of functional applications. By addressing and manipulating intracellular targets, these molecules hold great potential for treating cancer, respiratory diseases and neurological disorders, making this a vibrant area of research in the biomedical
Mariona Gené‐Verdés +2 more
wiley +1 more source

