Related papers: Terahertz Induced Protein Interactions in a Random…
For facile manipulation of polarization states of light for applications in communications, imaging, and information processing, an efficient mechanism is desired for rotating light polarization with a minimum interaction length. Here, we…
The intricate three-dimensional geometries of protein tertiary structures underlie protein function and emerge through a folding process from one-dimensional chains of amino acids. The exact spatial sequence and configuration of amino…
Conformational fluctuations are believed to play an important role in the process by which transcription factor proteins locate and bind their target site on the genome of a bacterium. Using a simple model, we show that the binding time can…
Protein sequences serve as a natural record of the evolutionary constraints that shape their functional structures. We show that it is possible to use only sequence information to go beyond predicting native structures and global stability…
A theoretical framework is developed to study the dynamics of protein folding. The key insight is that the search for the native protein conformation is influenced by the rate r at which external parameters, such as temperature, chemical…
Proteins must fold quickly to acquire their biologically functional three-dimensional native structures. Hence, these are mainly stabilized by local contacts, while intricate topologies such as knots are rare. Here, we reveal the existence…
PDZ (Post-synaptic density-95/discs large/zonula occludens-1) domains are relatively small (80 to 120 residues) protein binding modules central in the organization of receptor clusters and in the association of cellular proteins. Their main…
This paper considers a broadly biologically relevant question of a chain (such as a protein) binding to a sequence of receptors with matching multiple ligands distributed along the chain. This binding is critical in cell adhesion events,…
We systematically investigate the influence of annealing effect on terahertz (THz) generation from CoFeB based magnetic nanofilms driven by femtosecond laser pulses. Three times enhancement of THz yields are achieved in W/CoFeB through…
Protein folding cooperativity is defined by the nature of the finite-size thermodynamic transition exhibited upon folding: two-state transitions show a free energy barrier between the folded and unfolded ensembles, while downhill folding is…
For cellular functions like division and polarization, protein pattern formation driven by NTPase cycles is a central spatial control strategy. Operating far from equilibrium, no general theory links microscopic reaction networks and…
Flexible manipulation of terahertz-wave polarization during the generation process is very important for terahertz applications, especially for the next-generation on-chip functional terahertz sources. However, current terahertz emitters…
In this paper, the performance of a dual-hop relaying terahertz (THz) wireless communication system is investigated. In particular, the behaviors of the two THz hops are determined by three factors, which are the deterministic path loss,…
The combination of Terahertz (THz) and massive multiple-input multiple-output (MIMO) is promising to meet the increasing data rate demand of future wireless communication systems thanks to the huge bandwidth and spatial degrees of freedom.…
We conduct novel coverage probability analysis of downlink transmission in a three-dimensional (3D) terahertz (THz) communication (THzCom) system. In this system, we address the unique propagation properties in THz band, e.g., absorption…
Natural protein sequences contain a record of their history. A common constraint in a given protein family is the ability to fold to specific structures, and it has been shown possible to infer the main native ensemble by analyzing…
Living systems rely on coordinated molecular interactions, especially those related to gene expression and protein activity. The Unfolded Protein Response is a crucial mechanism in eukaryotic cells, activated when unfolded proteins exceed a…
The protein dynamical transition is investigated as a function of protein structure using terahertz time domain spectroscopy (THz-TDS). Measurements performed for native state and denatured hen egg white lysozyme (HEWL) show that protein…
Many native structures of proteins accomodate complex topological motifs such as knots, lassos, and other geometrical entanglements. How proteins can fold quickly even in the presence of such topological obstacles is a debated question in…
Extensive Monte Carlo folding simulations for four proteins of various structural classes are carried out, using a single atomistic potential. In all cases, collapse occurs at a very early stage, and proteins fold into their native-like…