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The triple helix model of innovation, as theorized by Etzkowitz and Leydesdorff, is based on the interactions between the three following elements and their associated 'initial role': [9] universities engaging in basic research, industries producing commercial goods and governments that are regulating markets. [2]
The collagen triple helix is a triple helix formed from three separate protein helices, spiraling around the same axis. In the fields of geometry and biochemistry, a triple helix (pl.: triple helices) is a set of three congruent geometrical helices with the same axis, differing by a translation along the axis. This means that each of the ...
Triple-stranded DNA (also known as H-DNA or Triplex-DNA) is a DNA structure in which three oligonucleotides wind around each other and form a triple helix. In triple-stranded DNA, the third strand binds to a B-form DNA (via Watson–Crick base-pairing) double helix by forming Hoogsteen base pairs or reversed Hoogsteen hydrogen bonds.
The quadruple and quintuple innovation helix framework was co-developed by Elias G. Carayannis and David F.J. Campbell, with the quadruple helix being described in 2009 [3] [4] and the quintuple helix in 2010. [4] [5] Various authors were exploring the concept of a quadruple helix extension to the triple helix model of innovation around the ...
Base triads in a DNA triple helix structure. This non-Watson–Crick base-pairing allows the third strands to wind around the duplexes, which are assembled in the Watson–Crick pattern, and form triple-stranded helices such as (poly(dA)•2poly(dT)) and (poly(rG)•2poly(rC)). [5]
In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.
The collagen protein is composed of a triple helix, which generally consists of two identical chains (α1) and an additional chain that differs slightly in its chemical composition (α2). [23] The amino acid composition of collagen is atypical for proteins, particularly with respect to its high hydroxyproline content.
In a triple-helix model (specifically Pauling and Corey's model), some of the van der Waals distances appear to be too small. The initial double helix model discovered, now termed B-form DNA is by far the most common conformation in cells. [12]