Sequence of Events during Peptide Unbinding from RNase S: A Complete Experimental Description

نویسندگان

چکیده

The phototriggered unbinding of the intrinsically disordered S-peptide from RNase S complex is studied with help transient IR spectroscopy, covering a wide range time scales 100 ps to 10 ms. To that end, an azobenzene moiety has been linked in way its helicity disrupted by light, thereby initiating complete unbinding. full sequence events observed, starting unfolding helical structure on 20 ns scale while still being binding pocket S-protein, after 300 μs, and structural response S-protein 3 With regard dynamics, mechanism can be classified as induced fit, better described conformational selection.

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Reconstitution of fully active RNase S by carboxypeptidase-degraded RNase S-peptide.

In attempting to relate the covalent structure of ribonuclease to its enzymic activity, controlled proteolytic degradation is a useful approach. Although native ribonuclease is markedly resistant to a variety of proteolytic enzymes, the separated components of ribonuclease S (1, 2), S-peptide, and S-protein, are extensively degraded by carboxypeptidase. Previous studies (3) on the sequence of a...

متن کامل

Complete Genomic Sequence of a Strain of Tomato Yellow Leaf Curl Virus from Iran

Background and Aims: Tomato yellow leaf curl virus (TYLCV) is one of the most destructive viruses of tomato that leads to reduced tomato yield up to 100% in tropical and subtropical regions. In this study, the complete sequence of TYLCV isolate from Hormozgan province, Iran and its recombination evsent was determined. Methods: TYLCV infected tomato was collected from Hormozgan province. Total D...

متن کامل

Neuropeptide Y: complete amino acid sequence of the brain peptide.

The amino acid sequence of neuropeptide Y, a 36-residue peptide recently isolated from porcine brain, has been determined by using high performance liquid chromatography for separation of its tryptic and chymotryptic fragments and subsequent sequence analysis of the isolated fragments by an improved dansyl Edman subtractive technique. The amino acid sequence of neuropeptide Y has been found to ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Journal of Physical Chemistry Letters

سال: 2021

ISSN: ['1948-7185']

DOI: https://doi.org/10.1021/acs.jpclett.1c01155