<p>The X and Y letters refer to the consensus sequence pattern (Gly-X-Y)<i><sub>n</sub></i> characteristic of collagen triple-helical domains. The numbers indicate percentage occupation of the X or Y position by a given amino acid type.</p>*<p>Excluding EPclPs from bacteriophages.</p>†<p>Include molecules such as C1q, mannose binding proteins, collectins, macrophage scavenger receptors, or acetyl cholinesterase, which contain in their sequence a collagen domain but are not formally classified as collagen types.</p
<p>Protein sequences of four types or groups of M proteins that harbored a prototypical PARF motif b...
<p>(<b>A</b>) Domain architectures. The collagen triple helical domains are labelled “Col”, and doma...
Understanding the structure, folding, and stability of collagen is complex because of its length and...
Collagens are extended trimeric proteins composed of the repetitive sequence glycine-X-Y. A (c) unde...
Collagens are the most abundant proteins in mammals. The collagen family comprises 28 members that c...
The primary structure of collagen is characterized by the repeating tripeptide sequence (Gly-R2-R3)n...
The analysis of factors contributing to the stability of proteins is a subject of intense debate. Pa...
The primary structure of collagen is characterized by the repeating tripeptide sequence (Gly-R<SUB>2...
Collagens contain sequence- and conformation-dependent epitopes responsible for their digestion by c...
Fibrillar collagens are the principal structural molecules of connective tissues. The assembly of co...
Sequences with glycine in every third position have been detected in DNA derived sequences of protei...
tripeptide sequence pattern suggest a physical basis for their differential susceptibility to matrix...
AbstractA sequence comparison of the C-termini of collagens X, VIII, the collagen-like complement fa...
Collagens are a large family of triple helical proteins that are widespread throughout the body and ...
The most abundant member of the collagen protein family, collagen I (COL1), is composed of two simil...
<p>Protein sequences of four types or groups of M proteins that harbored a prototypical PARF motif b...
<p>(<b>A</b>) Domain architectures. The collagen triple helical domains are labelled “Col”, and doma...
Understanding the structure, folding, and stability of collagen is complex because of its length and...
Collagens are extended trimeric proteins composed of the repetitive sequence glycine-X-Y. A (c) unde...
Collagens are the most abundant proteins in mammals. The collagen family comprises 28 members that c...
The primary structure of collagen is characterized by the repeating tripeptide sequence (Gly-R2-R3)n...
The analysis of factors contributing to the stability of proteins is a subject of intense debate. Pa...
The primary structure of collagen is characterized by the repeating tripeptide sequence (Gly-R<SUB>2...
Collagens contain sequence- and conformation-dependent epitopes responsible for their digestion by c...
Fibrillar collagens are the principal structural molecules of connective tissues. The assembly of co...
Sequences with glycine in every third position have been detected in DNA derived sequences of protei...
tripeptide sequence pattern suggest a physical basis for their differential susceptibility to matrix...
AbstractA sequence comparison of the C-termini of collagens X, VIII, the collagen-like complement fa...
Collagens are a large family of triple helical proteins that are widespread throughout the body and ...
The most abundant member of the collagen protein family, collagen I (COL1), is composed of two simil...
<p>Protein sequences of four types or groups of M proteins that harbored a prototypical PARF motif b...
<p>(<b>A</b>) Domain architectures. The collagen triple helical domains are labelled “Col”, and doma...
Understanding the structure, folding, and stability of collagen is complex because of its length and...