Primary structure separation

Conformational and phase transitions can potentially be indicative of the primary structure of thermosensitive macromolecules. Indeed, depending on the relative location of H- and P-blocks, as well as on the variation of their length, the chains can either undergo conformational transition accompanied by phase separation, or they can exhibit only the conformational changes without macroscopic phase transitions, i.e. the behaviour observed in the case of protein-like HP-copolymers. Therefore, the solution behaviour of separated fractions of these NVCl/NVIAz-copolymers in an aqueous medium at different temperatures is very important. 

In the primary structure of alternating block-copolymers the hydrophobic H-type blocks could be too short to facilitate the efficient cooperative hydrophobic interactions responsible for promoting the phase separation. 

ACh was first proposed as a mediator of cellular function by Hunt in 1907, and in 1914 Dale [2] pointed out that its action closely mimicked the response of parasympathetic nerve stimulation (see Ch. 10). Loewi, in 1921, provided clear evidence for ACh release by nerve stimulation. Separate receptors that explained the variety of actions of ACh became apparent in Dale s early experiments [2]. The nicotinic ACh receptor was the first transmitter receptor to be purified and to have its primary structure determined [3, 4]. The primary structures of most subtypes of both nicotinic and muscarinic receptors, the cholinesterases (ChE), choline acetyltransferase (ChAT), the choline and ACh transporters have been ascertained. Three-dimensional structures for several of these proteins or surrogates within the same protein family are also known. 

A series of separate SDOF dynamic analyses are performed for each of the primary structural components. For example, a typical roof system consists of a roof slab supported on structural steel roof beams which are in turn supported by roof girders. Separate SDOF dynamic analyses are performed for the slab, beams and girders using the reaction time history of the supported member as loading input 10... 

The polymer level is reached with the polypeptide chain, a long (usually 20+) chain of amino acids. A protein consists of one or more polypeptide chains. For proteins with only one chain, the chain is the protein. For multiple-chain proteins, known as oligomeric proteins, the polypeptide chain and protein levels must be viewed separately. Each different polypeptide chain has its own unique primary structure. 

As metabolic pathways became clearer, the detailed study of the enzymes involved was facilitated by the introduction of new procedures for isolation, purification, and characterization of proteins. Developments in chromatography in the early 1940s and the introduction of gel electrophoresis allowed more efficient methods to be used to separate proteins and to analyze their primary structure, so that Sanger was able, by 1953, to report the primary structure of insulin (Chapter 10). 

Primary structures of [NiFe] hydrogenases belonging to separate subclasses... 

I IFNs because they share a 30% sequence homology in their primary amino acid structure. IFN-y is structurally separate and is a Type II IFN. Type I IFNs are acid stable Type... 

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