TY - JOUR
T1 - Crystal and molecular structure of tert. ‐butyloxycarbonyl‐L‐prolyl‐α‐aminoisobutyryl‐L‐alanyl‐α‐aminoisobutyrate methyl ester
AU - van ROEY, PATRICK
AU - SMITH, G. DAVID
AU - BALASUBRAMANIAN, T. M.
AU - CZERWINSKI, E. W.
AU - MARSHALL, GARLAND R.
AU - MATHEWS, F. SCOTT
PY - 1983/10
Y1 - 1983/10
N2 - Boc‐Pro‐Aib‐Ala‐Aib‐OMe crystallizes in the orthorhombic space group P21212 with cell dimensions a = 17.701 (3)Å, b = 17.476 (4)Å, c = 9.686 (2)Å, V = 2996.3 Å3. The first three residues form a single turn of a 310‐helix stabilized by two intramolecular hydrogen bonds. Comparison of the conformation of the methyl ester of the tetrapeptide with that of its benzyl ester shows differences in the individual torsion angles of up to 29°, although the overall conformation is conserved.
AB - Boc‐Pro‐Aib‐Ala‐Aib‐OMe crystallizes in the orthorhombic space group P21212 with cell dimensions a = 17.701 (3)Å, b = 17.476 (4)Å, c = 9.686 (2)Å, V = 2996.3 Å3. The first three residues form a single turn of a 310‐helix stabilized by two intramolecular hydrogen bonds. Comparison of the conformation of the methyl ester of the tetrapeptide with that of its benzyl ester shows differences in the individual torsion angles of up to 29°, although the overall conformation is conserved.
KW - 3‐helix
KW - X‐ray diffraction
KW - peptide conformation
KW - α‐aminoisobutyrate
UR - http://www.scopus.com/inward/record.url?scp=0020835916&partnerID=8YFLogxK
U2 - 10.1111/j.1399-3011.1983.tb02109.x
DO - 10.1111/j.1399-3011.1983.tb02109.x
M3 - Article
C2 - 6654587
AN - SCOPUS:0020835916
VL - 22
SP - 404
EP - 409
JO - International Journal of Peptide and Protein Research
JF - International Journal of Peptide and Protein Research
SN - 0367-8377
IS - 4
ER -