Insertion of Pro-Hyp-Gly provides 2 kcal mol⁻¹ stability but attenuates the specific assembly of ABC heterotrimeric collagen triple helices

Abstract

Collagen is a major structural component of the extracellular matrix and connective tissue. The key structural feature of collagen is the collagen triple helix, with a Xaa-Yaa-Gly (glycine) repeating pattern....

Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps

“…Collagen model peptides (CMPs) with Pro‐Hyp‐Gly repeats have hence been used as synthetic surrogates. [1] These peptides consist typically of 20–40 amino acids and are useful for studying the factors that affect the stability[ 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 ] and the dynamics[ 20 , 21 , 22 , 23 , 24 ] of the collagen triple helix. Such studies revealed, for example, the importance of steric and stereoelectronic effects, interstrand H‐bonding, hydrophobicity, and PPII helicity of the individual strands for collagen triple helix stability.…”

Predicting Collagen Triple Helix Stability through Additive Effects of Terminal Residues and Caps

“…Collagen model peptides (CMPs) with Pro-Hyp-Gly repeats have hence been used as synthetic surrogates. [1] These peptides consist typically of 20-40 amino acids and are useful for studying the factors that affect the stability [7][8][9][10][11][12][13][14][15][16][17][18][19] and the dynamics [20][21][22][23][24] of the collagen triple helix. Such studies revealed, for example, the importance of steric and stereoelectronic effects, interstrand H-bonding, hydrophobicity, and PPII helicity of the individual strands for collagen triple helix stability.…”