Refined Folding Mechanism of a Helix-turn-helix Motif
نویسندگان
چکیده
منابع مشابه
Folding pathways of a helix-turn-helix model protein
A small model polypeptide represented in atomic detail is folded using Monte Carlo dynamics. The polypeptide is designed to have a native conformation similar to the central part of the helix-turn-helix protein ROP. Starting from a β-strand conformation or two different loop conformations of the protein glutamine synthetase, six trajectories are generated using the so-called window move in dihe...
متن کاملDNA recognition by proteins with the helix-turn-helix motif.
INTRODUCTION......... . ...... ................. .. ................. . .... . . ................. ......... 933 NOTIONS ABOUT RECOGNITION..... ................ . . .............. . . ..... . ......... . . ..... 934 THE HTH MOTIF... ..... ....... ................. .. . ................ .... . . .... ........... . .. . ..... .. 936 STRUCTURES.... . . . ..... .. ......... . . ................ ......
متن کاملHTHquery: a method for detecting DNA-binding proteins with a helix-turn-helix structural motif
SUMMARY HTHquery is a web-based service to determine if a protein structure has a helix-turn-helix structural motif which could bind to DNA. It is based on a similarity with a set of structural templates, the accessibility of a putative structural motif and a positive electrostatic potential in the neighbourhood of the putative motif. A set of scores are computed, based on each template, using ...
متن کاملStructure of bacteriophage phi29 head fibers has a supercoiled triple repeating helix-turn-helix motif.
The tailed bacteriophage 29 capsid is decorated with 55 fibers attached to quasi-3-fold symmetry positions. Each fiber is a homotrimer of gene product 8.5 (gp8.5) and consists of two major structural parts, a pseudohexagonal base and a protruding fibrous portion that is about 110 Å in length. The crystal structure of the C-terminal fibrous portion (residues 112-280) has been determined to a res...
متن کاملThe solution structure of the Mu Ner protein reveals a helix-turn-helix DNA recognition motif.
BACKGROUND The Mu Ner protein is a small (74 amino acids), basic, DNA-binding protein found in phage Mu. It belongs to a class of proteins, the cro and repressor proteins, that regulate the switch from the lysogenic to the lytic state of the phage life cycle. There is no significant sequence identity between Mu Ner and the cro proteins of other phages, despite their functional similarity. In ad...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2014
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2013.11.3716