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1.
The synthesis of the tetrapeptide benzyloxycarbonyl(α-aminoisobutyryl-L -prolyl)2-methyl ester (Z-(Aib-Pro)2-OMe) and an analysis of its conformation in solution and the solid state are reported. Stepwise synthesis using dicyclohexylcarbodiimide leads to racemization at Pro(2). Evidence for the presence of diastereomeric tetrapeptides is obtained from 270-MHz1H-nmr and 67.89-MHz 13C-nmr. The all-L tetrapeptide is obtained by fractional crystallization from ethyl acetate. The NH of Aib(3) is shown to be involved in an intramo-lecular hydrogen bond by variable-temperature 1H-nmr and the solvent dependence of NH chemical shifts. The results are consistent with a β-turn conformation with Aib(1) and Pro(2) at the corners stabilized by a 4 → 1 hydrogen bond. The molecule crystallizes in the space group P212121, with a = 8.839, b = 14.938, and c = 22.015 Å. The structure has been refined to an R value of 0.051. The peptide backbone is all-trans, and a 4 → 1 hydrogen bond, between the CO group of the urethane moiety and Aib(3) NH, is observed. Aib(1) and Pro(2) occupy the corner positions of a type I β-turn with ? = ?55.4°, Ψ = ?31.3° for Aib(1) and ? = ?71.6°, Ψ = ?38° for Pro(2). The tertiary amide unit linking Pro(2) and Aib(3) is significantly distorted from planarity (Δω = 14.3°). 相似文献
2.
B. V. Venkataram Prasad N. Shamala R. Nagaraj R. Chandrasekaran P. Balaram 《Biopolymers》1979,18(7):1635-1646
The crystal and molecular structure of N-benzyloxycarbonyl-α-aminoisobutyryl-L -prolyl methylamide, the amino terminal dipeptide fragment of alamethicin, has been determined using direct methods. The compound crystallizes in the orthorhombic system with the space group P212121. Cell dimensions are a = 7.705 Å, b = 11.365 Å, and c = 21.904 Å. The structure has been refined using conventional procedures to a final R factor of 0.054. The molecular structure possesses a 4 → 1 intramolecular N-H—O hydrogen bond formed between the CO group of the urethane moiety and the NH group of the methylamide function. The peptide backbone adopts the type III β-turn conformation, with ?2 = ?51.0°, ψ2 = ?39.7°, ?3 = ?65.0°, ψ3 = ?25.4°. An unusual feature is the occurrence of the proline residue at position 3 of the β-turn. The observed structure supports the view that Aib residues initiate the formation of type III β-turn conformations. The pyrrolidine ring is puckered in Cγ-exo fashion. 相似文献
3.
The crystal structure of (Z)-acetyl-α,β-dehydrophenylalanine methylamide (monoclinic Cc, a = 10.241(1), b = 15.252(1), c = 8.643(1) Å, β = 120.98(1)°, Z = 4) has been solved by x-ray diffraction to an R-factor = 0.148, and compared to that of the homologous L -phenylalanine dervative. Molecules are intermolecularly hydrogen-bonded to four neighboring molecules in a three-dimensional network with alternating layers of interacting amide bonds and orthogonally arranged phenyl rings. The existence of the Cα = Cβ double bond results in a phenyl orientation that is forbidden for phenylananine (χ1 = ?7,8°), and in shorter Cα ? Cβ and Cβ ? Cγ distances. The geometrical paramenters of the peptide backbone are not drastically modified by α,β-unsaturation. However, the N-Cα-C′ angle is increased by nearly 5°, and the dimensions, and therefore probably the electronic conjugation, of the N-terminal amide group to be affected by the occurrence of the vicinal Cα = Cβ double bond. 相似文献
4.
Naiem Ahmad Wani Rajni Kant Vivek Kumar Gupta Subrayashastry Aravinda Rajkishor Rai 《Journal of peptide science》2016,22(4):208-213
The present study describes the synthesis and crystallographic analysis of αγ hybrid peptides, Boc‐Gpn‐L‐Pro‐NHMe ( 1 ), Boc‐Aib‐Gpn‐L‐Pro‐NHMe ( 2 ), and Boc‐L‐Pro‐Aib‐Gpn‐L‐Pro‐NHMe ( 3 ). Peptides 1 and 2 adopt expanded 12‐membered (C12) helical turn over γα segment. Peptide 3 promotes the ribbon structure stabilized by type II β‐turn (C10) followed by the expanded C12 helical γα turn. Both right‐handed and left‐handed helical conformations for Aib residue are observed in peptides 2 and 3 , respectively Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd. 相似文献
5.
Yosuke Demizu Masakazu Tanaka Mitsunobu Doi Masaaki Kurihara Haruhiro Okuda Hiroshi Suemune 《Journal of peptide science》2010,16(11):621-626
A single chiral cyclic α,α‐disubstituted amino acid, (3S,4S)‐1‐amino‐(3,4‐dimethoxy)cyclopentanecarboxylic acid [(S,S)‐Ac5cdOM], was placed at the N‐terminal or C‐terminal positions of achiral α‐aminoisobutyric acid (Aib) peptide segments. The IR and 1H NMR spectra indicated that the dominant conformations of two peptides Cbz‐[(S,S)‐Ac5cdOM]‐(Aib)4‐OEt ( 1) and Cbz‐(Aib)4‐[(S,S)‐Ac5cdOM]‐OMe (2) in solution were helical structures. X‐ray crystallographic analysis of 1 and 2 revealed that a left‐handed (M) 310‐helical structure was present in 1 and that a right‐handed (P) 310‐helical structure was present in 2 in their crystalline states. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd. 相似文献
6.
K. Suguna S. Ramakumar N. Shamala B. V. Venkataram Prasad P. Balaram 《Biopolymers》1982,21(9):1847-1855
The crystal and molecular structures of two α-aminoisobutyric acid (Aib)-containing diketopiperazines, cyclo(Aib-Aib) 1 and cyclo(Aib-L -Ile) 2 , are reported. Cyclo(Aib-Aib) crystallizes in the space group P1 with a = 5.649(3), b = 5.865(2), c = 8.363(1), α = 69.89(6), β = 113.04(8), γ = 116.0(3), and Z = 1, while 2 occurs in the space group P212121 with a = 6.177(1), b = 10.791(1), c = 16.676(1), and Z = 4. The structures of 1 and 2 have been refined to final R factors of 0.085 and 0.086, respectively. In both structures the diketopiperazine ring shows small but significant deviation from planarity. A very flat chair conformation is adopted by 1, in which the Cα atoms are displaced by 0.07 Å on each side of the mean plane, passing through the other four atoms of the ring. Cyclo(Aib-Ile) favors a slight boat conformation, with Aib Cα and Ile Cα atoms displaced by 0.11 and 0.05 Å on the same side of the mean plane formed by the other ring atoms. Structural features in these two molecules are compared with other related diketopiperazines. 相似文献
7.
Some theoretical studies have predicted that the conformational freedom of the α-aminoisobutyric acid (H-Aib-OH) residue is restricted to the α-helical region of the Ramachandran map. In order to obtain conformational experimental data, two model peptide derivatives, MeCO-Aib-NHMe 1 and ButCO-LPro-Aib-NHMe 2 , have been investigated. The Aib dipeptide 1 crystallizes in the monoclinic system (a = 12.71 Å, b = 10.19 Å, c = 7.29 Å, β = 110.02°, Cc space group) and its crystal structure was elucidated by x-ray diffraction analysis. The azimuthal angles depicting the molecular conformation (? = ?55.5°, ψ = ?39.3°) fall in the α-helical region of the Ramachandran map and molecules are hydrogen-bonded in a three-dimensional network. In CCl4 solution, ir spectroscopy provides evidence for the occurrence of the so-called 5 and C7 conformers stabilized by the intramolecular i → i and i + 2 → i hydrogen bonds, respectively. The tripeptide 2 was studied in various solvents [CCl4, CD2Cl2, CDCl3, (CD3)2SO, and D2O] by ir and pmr spectroscopies. It was shown to accommodate predominantly the βII folded state stabilized by the i + 3 → i hydrogen bond. All these experimental findings indicate that the Aib residue displays the same conformational behavior as the other natural chiral amino acid residues. 相似文献
8.
John W. Perich Catherine L. Black N. Laila Huq Eric C. Reynolds 《Journal of peptide science》1999,5(5):221-233
The multiphosphorylated tryptic peptide αs1‐casein(59–79) has been shown to be antigenic with anti‐casein antibodies. In an approach to determine the amino acyl residues critical for antibody binding we undertook an epitope analysis of the peptide using overlapping synthetic peptides. With αs1‐casein(59–79) as the adsorbed antigen in a competitive ELISA only two of five overlapping synthetic peptides at 1 mM significantly inhibited binding of the anti‐casein antibodies. Peptides Glu‐Ser(P)‐Ile‐Ser(P)‐Ser(P)‐Ser(P)‐Glu‐Glu and Ile‐Val‐Pro‐Asn‐Ser(P)‐Val‐Glu‐Glu inhibited antibody binding by 20.0±3.6% and 60.3±7.9%, respectively. The epitope of Glu63‐Ser(P)‐Ile‐Ser(P)‐Ser(P)‐Ser(P)‐Glu‐Glu70 was further localised to the phosphoseryl cluster as the peptide Ser(P)‐Ser(P)‐Ser(P) significantly inhibited binding of the anti‐casein antibodies to αs1‐casein(59–79) by 29.5±7.4%. Substitution of Ser(P)75 with Ser75 in the second inhibitory peptide Ile‐Val‐Pro‐Asn‐Ser(P)75‐Val‐Glu‐Glu also abolished inhibition of antibody binding to αs1‐casein (59–79) demonstrating that Ser(P)75 is also a critical residue for recognition by the antibodies. These data show that the phosphorylated residues in the cluster sequence ‐Ser(P)66‐Ser(P)‐Ser(P)68 and in the sequence ‐Pro73‐Asn‐Ser(P)‐Val‐Glu77‐ are critical for antibody binding to αs1‐casein(59–79) and further demonstrate that a highly phosphorylated segment of a protein can be antigenic. Copyright © 1999 European Peptide Society and John Wiley & Sons, Ltd. 相似文献
9.
α,β-Dehydro amino acid residues are known to constrain the peptide backbone to the β-bend conformation. A pentapeptide containing only one α,β dehydrophenylalanine (ΔPhe) residue has been synthesized and crystallized, and its solid state conformation has been determined. The pentapeptide Boc-Leu-Phe-Ala-ΔPhe-Leu-OMe (C39H55N5O8, Mw = 721.9) was crystallized from aqueous methanol. Monoclinic space group was P21, a = 10.290(2)°, b = 17.149(2)°, c = 12.179(2) Å, β = 96.64(1)° with two molecules in the unit cell. The x-ray (Mo Kα, λ = 0.7107A) intensity data were collected using a CAD4 diffractometer. The crystal structure was determined by direct methods and refined using least-squares technique. R = 4.4% and Rw = 5.4% for 4403 reflections having |F0| ≥ 3σ(|F0|). All the peptide links are trans and the pentapeptide molecule assumes 310-helical conformation. The mean ?,ψ values, averaged over the first four residues, are ?64.4°, ?22.4° respectively. There are three 4 → 1 intramolecular hydrogen bonds, characteristic of 310,-helix. In the crystal, the peptide helices interact through two head-to-tail. N? H? O intermolecular hydrogen bonds. The peptide molecules related by 21, screw symmetry form a skewed assembly of helices. © 1995 John Wiley & Sons, Inc. 相似文献
10.
Isabelle Sgalas Yann Prigent Daniel Davoust Bernard Bodo Sylvie Rebuffat 《Biopolymers》1999,50(1):71-85
The three‐dimensional solution structure of harzianin HC IX, a peptaibol antibiotic isolated from the fungus Trichoderma harzianum, was determined using CD, homonuclear, and heteronuclear two‐dimensional nmr spectroscopy combined with molecular modeling. This 14‐residue peptide, Ac Aib1 Asn2 Leu3 Aib4 Pro5 Ala6 Ile7 Aib8 Pro9 Iva10 Leu11 Aib12 Pro13 Leuol14 (Aib, α‐aminoisobutyric acid; Iva, isovaline; Leuol, leucinol), is a main representative of a short‐sequence peptaibol class characterized by an acetylated N‐terminus, a C‐terminal amino alcohol, and the presence of three Aib‐L ‐Pro motifs at positions 4–5, 8–9, and 12–13, separated by two dipeptide units. In spite of a lower number of residues, compared to the 18/20‐residue peptaibols such as alamethicin, harzianin HC IX exhibits remarkable membrane‐perturbing properties. It interacts with phospholipid bilayers, increasing their permeability and forming voltage‐gated ion channels through a mechanism slightly differing from that proposed for alamethicin. Sequence‐specific 1H‐ and 13C‐nmr assignments and conformational nmr parameters (3JNHCαH coupling constants, quantitative nuclear Overhauser enhancement data, temperature coefficients of amide and carbonyl groups, NH–ND exchange rates) were obtained in methanol solution. Sixty structures were calculated based on 98 interproton distance restraints and 6 Φ dihedral angle restraints, using high temperature restrained molecular dynamics and energy minimization. Thirty‐seven out of the sixty generated structures were consistent with the nmr data and were convergent. The peptide backbone consists in a ribbon of overlapping β‐turns twisted into a continuous spiral from Asn2 to Leuol14 and forming a 26 Å long helix‐like structure. This structure is slightly amphipathic, with the three Aib–Pro motifs aligned on the less hydrophobic face of the spiral where the Asn2 side chain is also present, while the more hydrophobic bulky side chains of leucines, isoleucine, isovaline, and leucinol are located on the concave side. The repetitive (Xaa–Yaa–Aib–Pro) tetrapeptide subunit, making up the peptide sequence, is characterized by four sets of (Φ,Ψ) torsional angles, with the following mean values: Φi = −90°, Ψi = −27°; Φi+1 = −98°, Ψi+1 = −17°; Φi+2 = −49°, Ψi+2 = −50°; Φi+3 = −78°, Ψi+3 = +3°. We term this particular structure, specifically occurring in the case of (Xaa–Yaa–Aib–Pro)n sequences, the (Xaa–Yaa–Aib–Pro)‐β‐bend ribbon spiral. It is stabilized by 4 → 1 intramolecular hydrogen bonds and differs from both the canonical 310‐helix made of a succession of type III β‐turns and from the β‐bend ribbon spiral that has been described in the case of (Aib–Pro)n peptide segments. © 1999 John Wiley & Sons, Inc. Biopoly 50: 71–85, 1999 相似文献
11.
Kerstin Mhle Robert Günther Michael Thormann Norbert Sewald Hans‐Jrg Hofmann 《Biopolymers》1999,50(2):167-184
The conformation of oligomers of β‐amino acids of the general type Ac‐[β‐Xaa]n‐NHMe (β‐Xaa = β‐Ala, β‐Aib, and β‐Abu; n = 1–4) was systematically examined at different levels of ab initio molecular orbital theory (HF/6‐31G*, HF/3‐21G). The solvent influence was considered employing two quantum‐mechanical self‐consistent reaction field models. The results show a wide variety of possibilities for the formation of characteristic elements of secondary structure in β‐peptides. Most of them can be derived from the monomer units of blocked β‐peptides with n = 1. The stability and geometries of the β‐peptide structures are considerably influenced by the side‐chain positions, by the configurations at the Cα‐ and Cβ‐atoms of the β‐amino acid constituents, and especially by environmental effects. Structure peculiarities of β‐peptides, in particular those of various helix alternatives, are discussed in relation to typical elements of secondary structure in α‐peptides. © 1999 John Wiley & Sons, Inc. Biopoly 50: 167–184, 1999 相似文献
12.
Renate Gessmann Hans Brückner Michalis Aivaliotis Kyriacos Petratos 《Journal of peptide science》2015,21(6):476-479
The synthetic peptide Z‐Gly‐Aib‐Gly‐Aib‐OtBu was dissolved in methanol and crystallized in a mixture of ethyl acetate and petroleum ether. The crystals belong to the centrosymmetric space group P4/n that is observed less than 0.3% in the Cambridge Structural Database. The first Gly residue assumes a semi‐extended conformation (φ ±62°, ψ ?131°). The right‐handed peptide folds in two consecutive β‐turns of type II' and type I or an incipient 310‐helix, and the left‐handed counterpart folds accordingly in the opposite configuration. In the crystal lattice, one molecule is linked to four neighbors in the ab‐plane via hydrogen bonds. These bonds form a continuous network of left‐ and right‐handed molecules. The successive ab‐planes stack via apolar contacts in the c‐direction. An ethyl acetate molecule is situated on and close to the fourfold axis. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd. 相似文献
13.
To obtain general rules of peptide design using α,β-dehydro-residues, a sequence with two consecutive ΔPhe-residues, Boc-L -Val-ΔPhe–ΔPhe- L -Ala-OCH3, was synthesized by azlactone method in solution phase. The peptide was crystallized from its solution in an acetone/water mixture (70:30) in space group P61 with a=b=14.912(3) Å, c= 25.548(5) Å, V=4912.0(6) Å3. The structure was determined by direct methods and refined by a full matrix least-squares procedure to an R value of 0.079 for 2891 observed [I?3σ(I)] reflections. The backbone torsion angles ?1=?54(1)°, ψ1= 129(1)°, ω1=?177(1)°, ?2 =57(1)°, ψ2=15(1)°, ω2 =?170(1)°, ?3=80(1)°, ψ3 =7(2)°, ω3=?177(1)°, ?4 =?108(1)° and ψT4=?34 (1)° suggest that the peptide adopts a folded conformation with two overlapping β-turns of types II and III′. These turns are stabilized by two intramolecular hydrogen bonds between the CO of the Boc group and the NH of ΔPhe3 and the CO of Val1 and the NH of Ala4. The torsion angles of ΔPhe2 and ΔPhe3 side chains are similar and indicate that the two ΔPhe residues are essentially planar. The folded molecules form head-to- tail intermolecular hydrogen bonds giving rise to continuous helical columns which run parallel to the c-axis. This structure established the formation of two β-turns of types II and III′ respectively for sequences containing two consecutive ΔPhe residues at (i+2) and (i+3) positions with a branched β-carbon residue at one end of the tetrapeptide. 相似文献
14.
V. Pavone A. Lombardi M. Saviano B. Di Blasio F. Nastri R. Fattorusso L. Zaccaro O. Maglio T. Yamada Y. Omote S. Kuwata 《Biopolymers》1994,34(12):1595-1604
We report here the synthesis and molecular structure in the solid state of fully protected tripeptides containing Cα,α-diphenylglycine (Dph), namely Z-Aib-Dph-Gly-OMe (Aib: Cα,α-dimethylgrycine) and Bz-Dph-Dph-Gly-OMe. The molecular conformation around the Dph residue, containing two bulky substituents, is fully extended, while the Aib residue, containing two smaller groups on the Cα atom, adopts the typical 310/α-helical conformation. Gly residues, without substituents on the Cα atom, show different conformational preferences. Each residue seems to behave, from a conformational point of view, independently from the presence of the other residues, and thus mixed local conformations (folded and extended) are present in the crystals. The nonconventional peptide synthesis, using the Ugi reaction, is also reported. © 1994 John Wiley & Sons, Inc. 相似文献
15.
William J. Pestle Mark Hubbe Erin K. Smith Joseph M. Stevenson 《American journal of physical anthropology》2015,157(4):694-703
Objective : Development of a model for the prediction of δ13Cprotein from δ13Ccollagen and Δ13Cap‐co. Model‐generated values could, in turn, serve as “consumer” inputs for multisource mixture modeling of paleodiet. Methods : Linear regression analysis of previously published controlled diet data facilitated the development of a mathematical model for predicting δ13Cprotein (and an experimentally generated error term) from isotopic data routinely generated during the analysis of osseous remains (δ13Cco and Δ13Cap‐co). Results : Regression analysis resulted in a two‐term linear model (δ13Cprotein (%) = (0.78 × δ13Cco) ? (0.58× Δ13Cap‐co) ? 4.7), possessing a high R‐value of 0.93 (r2 = 0.86, P < 0.01), and experimentally generated error terms of ±1.9% for any predicted individual value of δ13Cprotein. This model was tested using isotopic data from Formative Period individuals from northern Chile's Atacama Desert. Conclusions : The model presented here appears to hold significant potential for the prediction of the carbon isotope signature of dietary protein using only such data as is routinely generated in the course of stable isotope analysis of human osseous remains. These predicted values are ideal for use in multisource mixture modeling of dietary protein source contribution. Am J Phys Anthropol 157:694–703, 2015. © 2015 Wiley Periodicals, Inc. 相似文献
16.
Three structurally different types of small peptides, namely, i) Boc‐Ile‐Aib‐Ile‐OMe (Aib=α‐aminoisobutyric acid), ii) Boc‐Xx‐m‐aminobenzoic acid (Xx=β‐Ala and γ‐aminobutyric acid), and iii) Boc‐Xx‐m‐nitroaniline, were found to exhibit β‐sheet‐mediated fibrillogenesis in the solid state, revealed by FT‐IR, single‐crystal X‐ray diffraction, and FE‐SEM studies. Interestingly, the fibrils grown from peptides 2 and 3 were found to bind with the physiological dye Congo red, a characteristic feature of amyloid fibrils. 相似文献
17.
Matthijs van der Knaap Fatih Basalan Henny C. van de Mei Henk J. Busscher Gijsbert A. van der Marel Herman S. Overkleeft Mark Overhand 《化学与生物多样性》2012,9(11):2494-2506
Via a Mannich reaction involving a dibenzyliminium species and the titanium enolates of Evans' chiral acylated oxazolidinones the β2‐amino acids (R)‐ and (S)‐Fmoc‐β2homovaline and (R)‐Fmoc‐β2homoleucine are synthesized. These building blocks were used, in combination with commercially available α‐ and β3‐amino acids, for the synthesis of the cyclo‐(αβ3αβ2α)2 peptide 2 and the cyclo‐(αβ2αβ3α)2 peptides 3 – 5 . The peptides 2 – 5 were screened for their ability to inhibit a small panel of Gram‐negative and Gram‐positive bacterial strains. 相似文献
18.
E. Benedetti V. Barone A. Bavoso B. Di Blasio F. Lelj V. Pavone C. Pedone G. M. Bonora C. Toniolo M. T. Leplawy K. Kaczmarek A. Redlinski 《Biopolymers》1988,27(3):357-371
Conformational energy computations on a derivative and a homo-dipeptide of Cα,α-diethylglycine were performed. In both cases the N- and C-terminal groups are blocked as acetamido and methylamido moieties, respectively. It was found that the Cα,α-diethylglycine residues are conformationally restricted and that the minimum energy conformation corresponds to the fully extended C5 structure when the N? Cα? C′ bond angle is smaller than 108° (as experimentally observed). The results of the theoretical analysis are in agreement with the crystal-state structural propensity of the complete series of N-trifluoroacetylated homo-peptides of this Cα,α-dialkylated residue from monomer to pentamer, determined by x-ray diffraction and also described in this work. Interestingly, for the first time, a crystallographically planar peptide backbone was observed (in the protected tripeptide). A comparison with peptides of Cα,α-dimethylglycine, Cα-methyl, Cα-ethylglycine, and Cα,α-di-n-propylglycine indicates that the fully extended conformation becomes more stable than the helical structures when both amino acid side-chain Cβ atoms are substituted. 相似文献
19.
Carlos Alemn 《Biopolymers》1994,34(7):841-847
A quantum mechanical study to compare the ability of α-aminoisobutyric acid (Aib), de-hydroalanine (ΔAla), and alanine (Ala) residues to stabilize helical conformations has been performed. To address the study, the oligopeptides Xn (X = Aib, ΔAla and Ala), where n varies from 1 to 6, were computed with the AM1 semiempirical method. The results show that the residues modified at the Cα carbon atom, Aib and ΔAla, are better helical formers than Ala. Thus, a cooperative energy effect was found for both residues, and especially for ΔAla. These terms permit the understanding the different conformational behaviors between Ala and its Cα-modified residues Aib and ΔAla. This trend is important for de novo protein design, where Aib and ΔAla must be considered useful residues in the design of synthetic helical motifs. © 1994 John Wiley & Sons, Inc. 相似文献
20.
Pivaloyl-L -Pro-Aib-N-methylamide has been shown to possess one intramolecular hydrogen bond in (CD3)2SO solution, by 1H-nmr methods, suggesting the existence of β-turns, with Pro-Aib as the corner residues. Theoretical conformational analysis suggests that Type II β-turn conformations are about 2 kcal mol?1 more stable than Type III structures. A crystallographic study has established the Type II β-turn in the solid state. The molecule crystallizes in the space group P21 with a = 5.865 Å, b = 11.421 Å, c = 12.966 Å, β = 97.55°, and Z = 2. The structure has been refined to a final R value of 0.061. The Type II β-turn conformation is stabilized by an intramolecular 4 → 1 hydrogen bond between the methylamide NH and the pivaloyl CO group. The conformational angles are ?Pro = ?57.8°, ψPro = 139.3°, ?Aib = 61.4°, and ψAib = 25.1°. The Type II β-turn conformation for Pro-Aib in this peptide is compared with the Type III structures observed for the same segment in larger peptides. 相似文献