Front Cover: β-Turn Mimicking Crosslinking Provides Hyperstability and Fast Folding Kinetics for Short Collagen Triple Helices (ChemBioChem 12/2025)

IF 2.6 4区生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY

ChemBioChem Pub Date : 2025-06-19 DOI:10.1002/cbic.202581201

Pengfei Jin, Diane N. Rafizadeh, Huanyi Zhao, Prof. David M. Chenoweth

引用次数: 0

Abstract

The image depicts the space-filling model of the constrained collagen mimetic peptide described in article 10.1002/cbic.202400834 by David M. Chenoweth and co-workers. Below it is a reflected image that reveals the peptide backbone structure. The terminal peptide loops glow in blue and red, highlighting the novel design of the β-turn–mimicking linker structures.

Abstract Image

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封面：β-转模拟交联提供超稳定性和快速折叠动力学的短胶原蛋白三螺旋（ChemBioChem 12/2025）

该图描绘了第10.1002/ cic号文章中描述的受限胶原模拟肽的空间填充模型。David M. Chenoweth及其同事的202400834。下面是显示肽主链结构的反射图像。末端肽环发出蓝色和红色的光，突出了β-转模拟连接体结构的新颖设计。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

ChemBioChem 生物-生化与分子生物学

CiteScore

6.10

自引率

3.10%

发文量

407

审稿时长

1 months

期刊介绍： ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).