Concerto™ Detachable Coil System - Medtronic
The Concerto™ Helix and 3D detachable coil systems offer helical and complex options for peripheral embolization. Concerto™ Helix is a soft coil in helical shape, designed for packing. It’s available in diameters from 2 to 20 millimeters. Concerto™ 3D is a conformable and stable coil in complex shape, designed for framing.
螺旋-线团转变 - 百度百科
螺旋-线团转变 [1]（ helix-coil transition ）是从a一螺旋构象向无 规线团的转变。 实验中可以在多肤的溶液中观察到C研究较 多的是合成的聚 u-基酸和标准的氨基酸的均聚物。 这种 转变可以通过改变溶剂的极性、氢键的强度、pH值和温度等 因素发生。 由此可以得到a-旋结构稳定性的信息. 螺旋-线团转变（ helix-coil transition ）是从a一螺旋构象向无 规线团的转变。
Helix–coil transition model - Wikipedia
Helix–coil transition models are formalized techniques in statistical mechanics developed to describe conformations of linear polymers in solution. The models are usually but not exclusively applied to polypeptides as a measure of the relative fraction of the molecule in an alpha helix conformation versus turn or random coil .
Concerto Detachable Coil Systems - Peripheral Embolization
Learn about Concerto Helix and 3D detachable coil systems for helical and complex options for peripheral embolization.
Coiled coil - Wikipedia
However, many other types of coiled coil exist. A coiled coil is a structural motif in proteins in which 2–7 [1] alpha-helices are coiled together like the strands of a rope. (Dimers and trimers are the most common types.) They have been found in roughly 5-10% of proteins and have a variety of functions. [2] .
18.1: Helix–Coil Transition - Chemistry LibreTexts
In evaluating the partition functions in helix–coil transition models, it is particularly useful to define a “statistical weight” for the helical configuration. It describes the influence of having an H on the probability of observing a particular configuration at kBT: s = e − Δϵ / kBT.
Recent advances in helix–coil theory - ScienceDirect
2002年12月10日 · The purpose of this review is to cover how helix–coil theories have been developed in the last 10 years, principally by including additional structural features of the helix, such as the distinct preferences that amino acids have for particular locations in the helix, or helix dipole interactions.
The Structure of α-Helical Coiled Coils - ScienceDirect
2005年1月1日 · α-Helical coiled coils are versatile protein domains, supporting a wide range of biological functions. Their fold is probably better understood than that of any other protein; indeed, uniquely among folds, their structure can be computed from a set of parametric equations.
Understanding a protein fold: The physics, chemistry, and biology …
2023年4月1日 · α-Helix and coiled-coil geometry. A, the α helix has a rise per residue (r) of 1.5 Å, 3.6 residues per helical turn, a backbone radius of 2.3 Å, and is stabilized by i CO to i + 4 NH hydrogen bonds. B, in Crick’s helical nets, the positions of the Cα atoms of an α helix, are projected as points onto a 2D plot (red).
From Helix–Coil Transitions to Protein Folding - PMC
An evolution of procedures to simulate protein structure and folding pathways is described. From an initial focus on the helix–coil transition and on hydrogen-bonding and hydrophobic interactions, our original attempts to determine protein structure and folding pathways were based on an experimental approach.
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