清晨好,您是今天最早来到科研通的研友!由于当前在线用户较少,发布求助请尽量完整的填写文献信息,科研通机器人24小时在线,伴您科研之路漫漫前行!

Integrated structural biology to unravel molecular mechanisms of protein-RNA recognition

核糖核酸 计算生物学 核糖核蛋白 RNA结合蛋白 生物 核酸结构 背景(考古学) 生物物理学 遗传学 基因 古生物学
作者
Andreas Schlundt,Jan‐Niklas Tants,Michael Sattler
出处
期刊:Methods [Elsevier BV]
卷期号:118-119: 119-136 被引量:51
标识
DOI:10.1016/j.ymeth.2017.03.015
摘要

Recent advances in RNA sequencing technologies have greatly expanded our knowledge of the RNA landscape in cells, often with spatiotemporal resolution. These techniques identified many new (often non-coding) RNA molecules. Large-scale studies have also discovered novel RNA binding proteins (RBPs), which exhibit single or multiple RNA binding domains (RBDs) for recognition of specific sequence or structured motifs in RNA. Starting from these large-scale approaches it is crucial to unravel the molecular principles of protein-RNA recognition in ribonucleoprotein complexes (RNPs) to understand the underlying mechanisms of gene regulation. Structural biology and biophysical studies at highest possible resolution are key to elucidate molecular mechanisms of RNA recognition by RBPs and how conformational dynamics, weak interactions and cooperative binding contribute to the formation of specific, context-dependent RNPs. While large compact RNPs can be well studied by X-ray crystallography and cryo-EM, analysis of dynamics and weak interaction necessitates the use of solution methods to capture these properties. Here, we illustrate methods to study the structure and conformational dynamics of protein-RNA complexes in solution starting from the identification of interaction partners in a given RNP. Biophysical and biochemical techniques support the characterization of a protein-RNA complex and identify regions relevant in structural analysis. Nuclear magnetic resonance (NMR) is a powerful tool to gain information on folding, stability and dynamics of RNAs and characterize RNPs in solution. It provides crucial information that is complementary to the static pictures derived from other techniques. NMR can be readily combined with other solution techniques, such as small angle X-ray and/or neutron scattering (SAXS/SANS), electron paramagnetic resonance (EPR), and Förster resonance energy transfer (FRET), which provide information about overall shapes, internal domain arrangements and dynamics. Principles of protein-RNA recognition and current approaches are reviewed and illustrated with recent studies.
最长约 10秒,即可获得该文献文件

科研通智能强力驱动
Strongly Powered by AbleSci AI
科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
8秒前
方白秋完成签到,获得积分10
15秒前
51秒前
54秒前
Sunny完成签到,获得积分10
1分钟前
2分钟前
Arthur Zhu发布了新的文献求助10
2分钟前
2分钟前
田様应助Arthur Zhu采纳,获得10
2分钟前
刘丰完成签到 ,获得积分10
2分钟前
mmmxxxx完成签到,获得积分10
3分钟前
无奈的萍完成签到,获得积分10
3分钟前
4分钟前
shi123发布了新的文献求助10
4分钟前
李健的小迷弟应助shi123采纳,获得10
4分钟前
shlw完成签到,获得积分10
4分钟前
路过完成签到 ,获得积分10
5分钟前
huangzsdy完成签到,获得积分10
5分钟前
沉默的友安完成签到 ,获得积分10
5分钟前
keyan完成签到 ,获得积分10
5分钟前
7分钟前
7分钟前
上官若男应助科研通管家采纳,获得10
7分钟前
7分钟前
shi123发布了新的文献求助10
7分钟前
shi123完成签到,获得积分20
7分钟前
连安阳完成签到,获得积分10
7分钟前
广阔天地完成签到 ,获得积分10
8分钟前
习月阳完成签到,获得积分10
8分钟前
8分钟前
jasmine完成签到 ,获得积分10
8分钟前
9分钟前
LZQ完成签到,获得积分0
10分钟前
可爱茹嫣完成签到,获得积分10
10分钟前
白嫖论文完成签到 ,获得积分10
10分钟前
不秃燃的小老弟完成签到 ,获得积分10
10分钟前
科研通AI2S应助科研通管家采纳,获得10
11分钟前
杪夏二八完成签到 ,获得积分10
11分钟前
12分钟前
科研通AI5应助丸橙采纳,获得30
12分钟前
高分求助中
Applied Survey Data Analysis (第三版, 2025) 800
Narcissistic Personality Disorder 700
The Martian climate revisited: atmosphere and environment of a desert planet 500
Plasmonics 400
建国初期十七年翻译活动的实证研究. 建国初期十七年翻译活动的实证研究 400
Towards a spatial history of contemporary art in China 400
Ecology, Socialism and the Mastery of Nature: A Reply to Reiner Grundmann 300
热门求助领域 (近24小时)
化学 材料科学 医学 生物 工程类 有机化学 物理 生物化学 纳米技术 计算机科学 化学工程 内科学 复合材料 物理化学 电极 遗传学 量子力学 基因 冶金 催化作用
热门帖子
关注 科研通微信公众号,转发送积分 3847806
求助须知:如何正确求助?哪些是违规求助? 3390526
关于积分的说明 10561646
捐赠科研通 3110862
什么是DOI,文献DOI怎么找? 1714585
邀请新用户注册赠送积分活动 825289
科研通“疑难数据库(出版商)”最低求助积分说明 775467