Abstract
Ab initio computations have been carried out during the past several years on diamides of single amino acids (HCO-NHCHR-CONH2 where R=H (glycine), -CH3 (alanine), -CH(CH3)2 (valine) and -CH2OH (serine)) exploring all possible backbone and side chain conformations. Selected conformations were studied in our laboratory on threonine (R=CH(CH3)OH), cystein (R=CH2-SH) and phenylalanine (R=CH2-C5H6) diamides. Tri-, tetra-, penta-, hexa- and hepta-amide systems of poly-L-alanine (H-(CONH-CHCH3-CONH)n-H 2 ≤n ≤ 6) were also investigated at selected backbone conformations. All these studies confirmed the results of multidimensional conformation analyses: the ith amino acid residue in a polypeptide has a maximum of nine (9) discrete backbone conformations. These structures correspond to nine conformational centres on the 2D-Ramachandran map. On the basis of this finding, it can be shown that the folded secondary structure of any protein with known internal coordinates, can be described in terms of these nine discrete conformation types.
| Original language | English |
|---|---|
| Pages (from-to) | 127-168 |
| Number of pages | 42 |
| Journal | International Reviews in Physical Chemistry |
| Volume | 14 |
| Issue number | 1 |
| Publication status | Published - 1995 |
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ASJC Scopus subject areas
- Physical and Theoretical Chemistry
Cite this
Searching for the simplest structural units to describe the three-dimensional structure of proteins. / Perczel, A.; Csizmadia, I.
In: International Reviews in Physical Chemistry, Vol. 14, No. 1, 1995, p. 127-168.Research output: Article
}
TY - JOUR
T1 - Searching for the simplest structural units to describe the three-dimensional structure of proteins
AU - Perczel, A.
AU - Csizmadia, I.
PY - 1995
Y1 - 1995
N2 - Ab initio computations have been carried out during the past several years on diamides of single amino acids (HCO-NHCHR-CONH2 where R=H (glycine), -CH3 (alanine), -CH(CH3)2 (valine) and -CH2OH (serine)) exploring all possible backbone and side chain conformations. Selected conformations were studied in our laboratory on threonine (R=CH(CH3)OH), cystein (R=CH2-SH) and phenylalanine (R=CH2-C5H6) diamides. Tri-, tetra-, penta-, hexa- and hepta-amide systems of poly-L-alanine (H-(CONH-CHCH3-CONH)n-H 2 ≤n ≤ 6) were also investigated at selected backbone conformations. All these studies confirmed the results of multidimensional conformation analyses: the ith amino acid residue in a polypeptide has a maximum of nine (9) discrete backbone conformations. These structures correspond to nine conformational centres on the 2D-Ramachandran map. On the basis of this finding, it can be shown that the folded secondary structure of any protein with known internal coordinates, can be described in terms of these nine discrete conformation types.
AB - Ab initio computations have been carried out during the past several years on diamides of single amino acids (HCO-NHCHR-CONH2 where R=H (glycine), -CH3 (alanine), -CH(CH3)2 (valine) and -CH2OH (serine)) exploring all possible backbone and side chain conformations. Selected conformations were studied in our laboratory on threonine (R=CH(CH3)OH), cystein (R=CH2-SH) and phenylalanine (R=CH2-C5H6) diamides. Tri-, tetra-, penta-, hexa- and hepta-amide systems of poly-L-alanine (H-(CONH-CHCH3-CONH)n-H 2 ≤n ≤ 6) were also investigated at selected backbone conformations. All these studies confirmed the results of multidimensional conformation analyses: the ith amino acid residue in a polypeptide has a maximum of nine (9) discrete backbone conformations. These structures correspond to nine conformational centres on the 2D-Ramachandran map. On the basis of this finding, it can be shown that the folded secondary structure of any protein with known internal coordinates, can be described in terms of these nine discrete conformation types.
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M3 - Article
AN - SCOPUS:0000063285
VL - 14
SP - 127
EP - 168
JO - International Reviews in Physical Chemistry
JF - International Reviews in Physical Chemistry
SN - 0144-235X
IS - 1
ER -