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For the biosensor application of the E / K coiled-coil the involvement of Dr. Maureen O Connor-McCourt Dr. 6 one strand of the heterodimeric coiled-coil e.g. K peptide is rst covalently attached to the biosensor surface. B 715 1998 307 329 3. 4. The use of E / K coiled-coil for biosensor applications. 3. 5. A heterodimeric coiled-coil af nity matrix protein tag system. 6. Utility of the E / K heterodimerization domain for biosensor experiments. .

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Groups of amino acids within the protein can then fold into three-dimensional shapes, one of the most common being a helical structure known as an α-helix. Two or more α-helices may be wound around each other to form a bundle called a coiled coil, which is found in many proteins.

Examples of proteins with coiled coil regions include myosins, tropomyosins and intermediate filaments. In UniProtKB/Swiss-Prot, we annotate coiled coils predicted using the COILS program of Lupas. The minimum size for predicted coiled coils is 28 amino acids.

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.)

3.2. Coiled coils are formed when two or more α-helices self-assemble by winding around each other to form a left-handed supercoil (Fig. 3.1C). Although dimers, trimers, and tetramers are the most common structures, larger coiled-coils of up to seven helices can now be prescriptively designed [8].

Coiled‐coil proteins mediate vesicle tethering The coiled‐coil domain functions as a spacer of approximately 0.5 µm between a short non‐coil sequence at its N‐terminus that binds the Golgi and a C‐terminal transmembrane segment that captures vesicles.

A coiled-coil or superhelix is formed by coiling two, three or four α-helices together. The helical strands are held together by the hydrophobic force formed between nonpolar side chains from the different peptide strands.

Examples of proteins with coiled coil regions include myosins, tropomyosins and intermediate filaments. In UniProtKB/Swiss-Prot, we annotate coiled coils predicted using the COILS program of Lupas. The minimum size for predicted coiled coils is 28 amino acids.

Coiled coils are formed when two or more α-helices self-assemble by winding around each other to form a left-handed supercoil (Fig. 3.1C). Although dimers, trimers, and tetramers are the most common structures, larger coiled-coils of up to seven helices can now be prescriptively designed [8].

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Form Packages
Adoption
Bankruptcy
Contractors
Divorce
Home Sales
Employment
Identity Theft
Incorporation
Landlord Tenant
Living Trust
Name Change
Personal Planning
Small Business
Wills & Estates
Packages A-Z
Form Categories
Affidavits
Bankruptcy
Bill of Sale
Corporate - LLC
Divorce
Employment
Identity Theft
Internet Technology
Landlord Tenant
Living Wills
Name Change
Power of Attorney
Real Estate
Small Estates
Wills
All Forms
Forms A-Z
Form Library
Customer Service
Terms of Service
DMCA Policy
About Us
Blog
Affiliates
Contact Us
Privacy Notice
Delete My Account
Site Map
All Forms
Search all Forms
Industries
Forms in Spanish
Localized Forms
Legal Guides
Real Estate Handbook
All Guides
Prepared for You
Notarize
Incorporation services
Our Customers
For Consumers
For Small Business
For Attorneys
Our Sites
US Legal Forms
USLegal
FormsPass
pdfFiller
signNow
airSlate workflows
DocHub
Instapage
Social Media
Call us now toll free:
1-877-389-0141
As seen in:
  • USA Today logo picture
  • CBC News logo picture
  • LA Times logo picture
  • The Washington Post logo picture
  • AP logo picture
  • Forbes logo picture
© Copyright 1997-2025
airSlate Legal Forms, Inc.
3720 Flowood Dr, Flowood, Mississippi 39232