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Protocol Thiol-based site-specific and covalent immobilization of biomolecules for single-molecule experiments Julia L Zimmermann1 2 Thomas Nicolaus1 Gregor Neuert1 3 Kerstin Blank1 4 Lehrstuhl f r Angewandte Physik Center for Nanoscience LMU M nchen M nchen Germany.

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Thiol-based antioxidant enzymes To prevent the uncontrolled oxidative modification of proteins, lipids and DNA and protect cells against irreversible and toxic damage, cells evolved a number of highly efficient and specific antioxidant enzymes. Superoxide dismutase catalyzes the conversion of O 2 • − into H2O2 and O2.

A sulfhydryl group (also called “thiol group”) consists of a sulfur atom with two lone pairs, bonded to hydrogen. The sulfhydryl group is ubiquitous in our body and mostly found in the oxidized form as disulfide linkages. The disulfide linkages contribute to the tertiary and quaternary structures of proteins.

Surface immobilization provides a useful platform for biosensing, drug screening, tissue engineering and other chemical and biological applications. However, some of the used reactions are inefficient and/or complicated, limiting their applications in immobilization.

Thiols are typically detected directly by virtue of their relatively high reactivity compared to most other common species in biological systems. Disulfides, on the other hand, have no strong chemical signature, and are hence most commonly detected after reduction to their corresponding thiols.

There are three major methods for immobilizing biomolecules: physical adsorption; physical “entrapment;” and covalent attachment (Stark, 1971; Zaborsky, 1973; Dunlap, 1974). Physical adsorption includes: (1) van der Waals interactions; (2) electrostatic interactions; and (3) affinity recognition.

Thiols are found in nature mainly in more complex combinations. Cysteine, for example is a common amino acid having an SH group. Volatile thiols are known for their strong odor. As an example, 1-butanethiol has an odor threshold of 6 ppb in water and a flavor threshold of 0.004 ppb.

A thiol group is a sulfur with a bonded hydrogen. Through an oxidation reaction, the sulfurs from two different cysteine amino acids can bond together to form a disulfide bridge. Methionine, the other sulfur containing amino acid, is incapable of forming disulfide bridges in biological systems.

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Living Trust
Name Change
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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
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Affiliates
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Privacy Notice
Delete My Account
Site Map
All Forms
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Industries
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Localized Forms
Legal Guides
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All Guides
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Notarize
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Our Sites
US Legal Forms
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FormsPass
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airSlate workflows
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As seen in:
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© Copyright 1997-2025
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