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2 edition of Coiled-coil assembly by proteins and peptides with unusual sequence motifs found in the catalog.

Coiled-coil assembly by proteins and peptides with unusual sequence motifs

Matthew Raymond Hicks

Coiled-coil assembly by proteins and peptides with unusual sequence motifs

by Matthew Raymond Hicks

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Published .
Written in English


Edition Notes

D.Phil. 2000. BLDSC DXN033017.

Statement[by] Matthew Raymond Hicks.
SeriesSussex theses ; S 4905
ID Numbers
Open LibraryOL18573492M

Coiled-coil peptides have proven useful in a range of materials applications ranging from the formation of well-defined fibrils to responsive hydrogels. The ability to design from first principles their oligomerization and subsequent higher order assembly offers their expanded use in . COILS is a program that compares a sequence to a database of known parallel two-stranded coiled-coils and derives a similarity score. By comparing this score to the distribution of scores in globular and coiled-coil proteins, the program then calculates the probability that the sequence will adopt a coiled-coil .

The α-helical coiled coil is a ubiquitous protein-folding motif found throughout all proteomes (Rackham et al. ) and in many proteins with diverse functions (Mason and Arndt ; Parry and Squire ).Though they occur within larger protein domains, the primary role of coiled coils is structural, and specifically to direct and cement protein–protein interactions in water-soluble. Keratin is a "coiled-coil" protein. Answer the following questions about keratin. or less good, about the other two possibilities? Question 5. (a) Using the table of AA propensities from the book, rate each of the three peptides below for its likelihood to be found in either an a-helix or a B-sheet, by adding up the values for each amino.

The coiled coil is a superhelical protein structural motif that consists of two or more alpha-helical peptides that are wrapped around each other in superhelical fashion. Coiled coils are amongst the most ubiquitous folding motifs found in proteins and have not only been identified in structural proteins but also play an important role in various intracellular regulation processes as well as. The first level is the amino acid sequence - there are 20 different amino acids most commonly found in proteins. The sequence of these amino acids in a polypeptide chain essentially determines the types of secondary structure elements present (the second level of organization) and the way by which they are arranged in space, creating structural.


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Coiled-coil assembly by proteins and peptides with unusual sequence motifs by Matthew Raymond Hicks Download PDF EPUB FB2

Coiled-coil assembly by peptides with non-heptad sequence motifs Matthew R Hicks1, David V Holberton2, Christopher Kowalczyk1 and Derek N Woolfson1 Background: The seven-residue heptad repeat is the accepted hallmark of coiled coils. In extended filamentous proteins.

Coiled-coil assembly by proteins and peptides with unusual sequence motifs. Author: Hicks, Matthew Raymond. Awarding Body: University of Sussex Current Institution: University of Sussex Date of Award: Availability of Full Text. The coiled coil is a ubiquitous protein-folding motif that guides oligomerization in a wide variety of systems, including transcription factors, muscle proteins, intermediate filaments and extracellular fibres.The sequences of all these proteins contain patterns of seven residues (heptads) in which hydrophobic sidechains are alternately spaced three and four residues by: Coiled-coils, the bundles of intertwined helical protein motifs, have drawn much attention as versatile molecular toolkits.

Because of programmable interaction specificity and affinity as well as well-established sequence-to-structure relationships, coiled-coils have been used as subunits that self-assemble various molecular complexes in a range of : Won Min Park.

The folding propensity of proteins and their assembly into higher order structures has inspired the design of minimal peptide folds and interaction motifs.

1 A prime example is the coiled‐coil structural motif, which has emerged as a powerful tool to assemble macromolecular architectures. 2 Coiled‐coils consist of at least two α‐helical peptides forming a super by: 3. The coiled coil is a superhelical protein structural motif that consists of two or more α-helical peptides that are wrapped around each other in superhelical fashion.

In recent years, the well-known coiled-coil motif has been widely employed in the generation of novel biomaterials. The canonical coiled-coil, comprised of two (or more) right-handed α-helices, is a left-handed super-helix wherein the constituent α-helices have a crossing angle (angle between two helices of a coiled-coil (Lupas ) of roughly 20° (Lupas and Gruber )).

The α-helical coiled coil (CC) is a common protein motif that because of the simplicity of its sequence/structure relationship, it has been studied extensively to address fundamental questions in. The TACC family of proteins include human TACC3, murine TACC3, human TACC2/AZU-1/ECTACC, human TACC1, D-TACC and murine AINT ().Members of this family of proteins are defined by the presence of the so-called TACC domain, a predicted coiled-coil region in their carboxyl terminus ().In fact, the TACC proteins show the most similarity in this region as they share very little sequence.

A coiled coil is a structural motif in proteins in which 2–7 alpha-helices are coiled together like the strands of a rope (dimers and trimers are the most common types). Many coiled coil-type proteins are involved in important biological functions such as the regulation of gene expression, e.g.

transcription e examples are the oncoproteins c-Fos and c-jun, as well as the muscle. Coiled-coil peptides are frequently used to create new function upon self-assembly of supramolecular complexes. A multitude of coil peptide sequences provides control over specificity and.

MOTIFS: USING DATABASES & CREATING YOUR OWN. SEARCHING MOTIF DATABASES. BACKGROUND INFORMATION: Proteins having related functions may not show overall high homology yet may contain sequences of amino acid residues that are highly conserved.

For background information on this see PROSITE at ExPASy. N.B. I recommend that you check your protein sequence with at. huntingtin protein, play a significant role in the kinetics of assembly specifically in polyglutamine-containing proteins.1,16 A sequence-mining survey by Kandel, Hendrickson, and others17 was conducted, and they found that predicted coiled-coil sequences proximal to polyglutamine sequences are quite common and thus are strongly implicated in.

The coiled coil is one of the most abundant protein structural motifs found in nature. It is especially common in fibrous proteins such as myosin.

Fletcher et al. published online 11 April; see the Perspective by Ardejani and Orner) designed two coiled-coil peptide motifs, a heterodimer, and a homotrimer. Both peptides contained. The coiled-coil protein oligomerization motif consists of two or more amphipathic alpha helices that twist around each other in a supercoil (Burkhard et al., ).

It was one of the earliest protein structures discovered, first described for the hair protein alpha keratin (Crick, ).

The coiled-coil was one of the earliest protein structures described and first discovered in the two-stranded coiled-coil protein alpha-keratin [].Coiled-coils consist of two or more alpha-helices winding around each other in a supercoil, a simple yet versatile protein fold [].Mutations in coiled-coil proteins have been implicated in a large variety of human diseases such as severe skin.

F ig Amino acid sequences of coiled-coil regions attached to the full-length type IIA procollagen N-propeptide. Fusion proteins were synthesized containing the human IIA N-propeptide fused to 18, 25, or 31 amino acids of the coiled-coil region from the human type II procollagen C-propeptide (IIA N-pro/CPII amino acids –, –, or –, respectively).

At the peptide is largely in a β-sheet conformation, consistent with that inferred from the ThT binding assay. It was interesting to note that on day 7 the peptide shows a decidedly α-helical character, suggesting the possibility that an intermediate in the aggregation pathway involves coiled-coil assembly, as proposed previously.

Self-assembly of designed coiled coil peptides studied by small-angle X-ray scattering and analytical ultracentrifugation Leila Malik,a Jesper Nygaard,a,b Niels J. Christensen,a Werner W. Streicher,c Peter W.

Thulstrup,a Lise Arletha and Knud J. Jensena* a-Helical coiled coil structures, which are noncovalently associated heptad repeat peptide sequences, are ubiquitous in nature. Signal-3L - is an online server for predicting the N-terminal protein signal peptide, and the input is the amino acid sequence only.

It is constructed with a hierarchical mixture model, which contains the following three layers: (1) Discrimination of SP (Signal Peptide) proteins and TMH (TransMembrane Helical) proteins from the other.Coiled-Coil Peptide Beacon:ATunable Conformational Switch for Protein Detection Carolin Mueller and ann* Abstract: The understanding of protein folding and assembly is of central importance for the design of proteins and enzymes with novel.

Sequence Properties of TAA Coiled Coils. The stalks of TAAs may extend for considerable distances and are rich in coiled-coil segments. The stalk of the Bartonella henselae adhesin BadA, for example, projects the head ≈ nm away from the cell surface and contains 23 coiled-coil segments along its 2, residue length ().Individual segments vary widely in size, from .