Revised and updated, Chemical Reagents for Protein Modification, Third Edition is an encyclopedic work describing the many approaches to the site-specific modification of …
Precise determination of disulfide linkages between cysteine (Cys) residues in proteins is essential in the determination of protein structure. Therefore, a reliable automated method …
RJ Souness, T Kleffmann, EP Tchesnokov… - Biochemistry, 2013 - ACS Publications
Describing the organization of substrates and substrate analogues in the active site of cysteine dioxygenase identifies potential intermediates in this critical yet poorly understood …
In contrast to other vertebrate hemoglobins (Hbs) whose high intrinsic O2 affinities are reduced by red cell allosteric effectors (mainly protons, CO2, organic phosphates, and …
JF Siebel, RL Kosinsky, B Åkerström, M Knipp - Chembiochem, 2012 - Wiley Online Library
Abstract α1‐Microglobulin (α1m) is a 26 kDa plasma and tissue protein belonging to the lipocalin protein family. Previous investigations indicate that the protein interacts with heme …
Nitrophorins represent a unique class of heme proteins that are able to perform the delicate transportation and release of the free-radical gaseous messenger nitric oxide (NO) in a pH …
S Abbruzzetti, C He, H Ogata, S Bruno… - Journal of the …, 2012 - ACS Publications
NO is an important signaling molecule in human tissue. However, the mechanisms by which this molecule is controlled and directed are currently little understood. Nitrophorins (NPs) …
C He, S Neya, M Knipp - Biochemistry, 2011 - ACS Publications
The factors leading to the breakage of the proximal iron–histidine bond in the ferroheme protein soluble guanylate cyclase (sGC) are still a matter of debate. This event is a key …
Nitric oxide signals through activation of soluble guanylyl cyclase (sGC), a heme-containing heterodimer. NO binds to the heme domain located in the N-terminal part of the β subunit of …